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Small-angle X-ray scattering

Small-angle X-ray scattering (SAXS) is a nondestructive analytical technique that quantifies nanoscale density differences in samples by measuring the intensity of X-rays scattered at very small angles, typically between 0.1° and 10°, corresponding to structural features from 1 to 100 nm or larger.^[1]^[2] The method provides low-resolution, ensemble-averaged information on the size, shape, conformation, and spatial organization of particles in their native environment, such as solutions or soft matter, without requiring crystallization or high concentrations.^[1]^[2] The fundamental principle of SAXS is based on the elastic scattering of X-rays by electrons in the sample, where the scattered waves interfere constructively or destructively depending on the electron density variations at the nanoscale.^[1] The scattering intensity I(q) is recorded as a function of the scattering vector q = (4π/λ) sin(θ/2), with λ as the X-ray wavelength and θ as half the scattering angle; small q values probe larger length scales.^[1]^[3] Analysis methods, such as the Guinier approximation for low-q regions to determine the radius of gyration R_g or pair distance distribution functions via Fourier transform, enable extraction of structural parameters like overall dimensions and internal heterogeneities.^[2] Modern implementations often combine SAXS with wide-angle X-ray scattering (WAXS) for multi-scale insights and leverage synchrotron or laboratory sources for time-resolved studies under varying conditions like temperature or pressure.^[3] SAXS originated in the early 20th century, with theoretical foundations laid by Peter Debye in 1915 on scattering from density fluctuations and André Guinier in 1939, who introduced approximations for dilute particle systems.^[2] The field was formalized in the 1955 book Small-Angle Scattering of X-Rays by Guinier and Gérard Fournet, which provided the mathematical framework for interpreting scattering patterns from colloidal and macromolecular systems.^[1]^[2] Significant advancements occurred in the 1970s with the advent of synchrotron radiation sources, enabling the first dedicated SAXS beamline in 1971 for dynamic biological studies like muscle contraction; subsequent improvements in detectors and beamlines from the 1990s onward facilitated routine time-resolved and in situ experiments.^[3] Over the last two decades, SAXS has become a cornerstone of structural molecular biology due to enhanced computational tools and access to high-brilliance sources.^[4] Applications of SAXS span diverse fields, including structural biology for characterizing flexible proteins, RNA complexes, and biomolecular assemblies in solution—such as hemoglobin folding or membrane protein conformations—where it complements high-resolution techniques like X-ray crystallography or NMR.^[2] In materials science, it investigates polymer dynamics, nanoparticle growth, and hierarchical structures in colloids or composites, often under operando conditions like deformation or chemical reactions.^[3]^[1] The technique's versatility extends to energy-related studies, such as biomineralization or soot formation in flames, and benefits from integration with molecular dynamics simulations for refined modeling of complex systems.^[2]^[1]

Fundamentals

Definition and Principles

Small-angle X-ray scattering (SAXS) is an analytical technique that utilizes the elastic scattering of X-rays at very small angles, typically in the range of 0.1 to 10 degrees, to quantify variations in electron density within a sample on length scales of 1 to 100 nanometers.^[1] This method enables the non-destructive investigation of nanoscale structures in materials ranging from soft matter to biological macromolecules, without requiring crystallization or long-range order in the sample.^[5] The physical basis of SAXS lies in the interaction of X-rays with matter through Thomson scattering, where the electric field of the incident X-ray beam accelerates electrons in the sample, causing them to re-emit spherical waves of the same wavelength.^[1] These scattered waves from different electrons interfere constructively or destructively depending on their relative phases, producing a scattering pattern that reflects the spatial distribution of electron density contrasts within the sample.^[5] The resulting intensity pattern encodes information about the size, shape, and organization of nanoscale features, such as particles, pores, or assemblies.^[6] In contrast to wide-angle X-ray scattering (WAXS), which probes atomic-scale structures on the order of angstroms by measuring scattering at larger angles, SAXS focuses on larger-scale electron density fluctuations accessible at low angles.^[1] The basic experimental setup involves directing a collimated, monochromatic X-ray beam onto the sample, often in transmission geometry, with the scattered radiation captured by a two-dimensional area detector positioned downstream to resolve the small-angle regime.^[5] A central concept in SAXS is the representation of scattering data in reciprocal space, where the scattering vector \mathbf{q} quantifies the momentum transfer from the incident to the scattered beam. The magnitude of q is given by

q = \frac{4\pi}{\lambda} \sin\left(\frac{\theta}{2}\right),

with \lambda as the X-ray wavelength and \theta as the scattering angle; low q values (e.g., 0.001 to 1 Å⁻¹) correspond to the nanoscale features probed by SAXS.^[1]

Historical Development

Small-angle X-ray scattering (SAXS) originated in the 1930s as a method to investigate nanoscale structures in materials, particularly precipitates in alloys. André Guinier, a French physicist, pioneered the technique during his PhD work at the University of Paris, publishing his seminal 1939 paper that derived the Guinier approximation for analyzing scattering from dilute particles, enabling the determination of particle size and shape from low-angle diffraction patterns.^[7] This early development built on initial observations of small-angle scattering reported as far back as 1930, but Guinier's contributions established SAXS as a distinct tool for studying heterogeneous materials without requiring crystalline order.^[8] The foundational text "Small-Angle Scattering of X-Rays" by André Guinier and Gérard Fournet, published in 1955, systematized the theory, experimental methods, and applications of SAXS, drawing from wartime and postwar research on metals and polymers.^[8] Post-World War II advancements in the 1960s and 1970s were driven by improved X-ray sources, including rotating anode generators, which enhanced flux and resolution for laboratory-based experiments.^[9] A major breakthrough occurred in the 1970s with the advent of synchrotron radiation sources, providing orders-of-magnitude brighter and more coherent beams that enabled higher signal-to-noise ratios and the initiation of time-resolved studies.^[10] The 1980s and 1990s saw the proliferation of dedicated synchrotron beamlines worldwide, facilitating brighter beams for dynamic processes such as phase transitions in materials and biological systems, with time-resolved SAXS becoming routine for capturing kinetics on millisecond timescales.^[11] Commercial SAXS instruments, such as the Kratky camera produced by Anton Paar, became available starting in the 1950s, stemming from efforts at Otto Kratky's Institute for Physical Chemistry in Graz, Austria, which democratized the technique beyond specialized facilities.^[9]^[12] In the 2000s, SAXS integrated with bioinformatics tools for protein structure determination, particularly for flexible macromolecules in solution, where hybrid modeling combined SAXS data with homology models and molecular dynamics to reconstruct low-resolution envelopes and conformational ensembles.^[13] Recent developments through 2025 have expanded SAXS applications in drug discovery, leveraging time-resolved measurements to screen small-molecule candidates and monitor binding dynamics in situ.^[14] Concurrently, X-ray free-electron lasers (XFELs) have enabled ultrafast, in situ studies of transient states in biomolecules and nanomaterials, achieving microsecond resolution for irreversible processes like protein folding and catalytic reactions.^[15]

Theory

Scattering Basics

Small-angle X-ray scattering (SAXS) is based on the elastic scattering of X-rays by matter, where the incident X-ray beam with wavevector \mathbf{k}_i interacts with the sample, producing a scattered beam with wavevector \mathbf{k}_f of the same magnitude |\mathbf{k}_i| = |\mathbf{k}_f| = 2\pi / \lambda, \lambda being the X-ray wavelength. The momentum transfer vector \mathbf{q} = \mathbf{k}_i - \mathbf{k}_f characterizes the scattering event, with magnitude q = (4\pi / \lambda) \sin(\theta / 2), where \theta is the scattering angle. This elastic process conserves energy, and in the small-angle regime, low q values probe large real-space distances on the order of nanometers to hundreds of nanometers.^[16] The scattering amplitude A(\mathbf{q}) arises from the coherent superposition of waves scattered by the electrons in the sample and is given by the Fourier transform of the electron density \rho(\mathbf{r}):

A(\mathbf{q}) = \int \rho(\mathbf{r}) \exp(i \mathbf{q} \cdot \mathbf{r}) \, d\mathbf{r},

where the integral extends over the illuminated sample volume. This expression derives from the Born approximation for weak scattering potentials, treating the sample as a collection of scatterers with density \rho(\mathbf{r}), each contributing a phase shift proportional to \exp(i \mathbf{q} \cdot \mathbf{r}). For a single particle or domain, A(\mathbf{q}) encodes the spatial arrangement of electrons within that structure.^[16] The measured scattering intensity I(\mathbf{q}) is the orientationally averaged modulus squared of the amplitude for isotropic samples, I(q) = \langle |A(\mathbf{q})|^2 \rangle, where the average \langle \cdot \rangle is over all orientations. Equivalently, I(q) represents the Fourier transform of the electron density pair correlation function \gamma(\mathbf{r}), defined as \gamma(\mathbf{r}) = \langle \rho(\mathbf{0}) \rho(\mathbf{r}) \rangle / \langle \rho \rangle^2 - 1, which quantifies the probability of finding electron density pairs separated by distance r. In practice, for systems of N particles, the total intensity decomposes as I(q) = N P(q) + N(N-1) |f(q)|^2 S(q), where P(q) = \langle |A(\mathbf{q})|^2 \rangle / |A(\mathbf{0})|^2 is the normalized form factor describing intra-particle scattering from shape and internal structure, and S(q) is the structure factor capturing inter-particle interferences due to interactions or correlations.^[17] Conventionally, q is expressed in reciprocal angstroms (Å⁻¹), reflecting the inverse length scale probed, while I(q) is reported in arbitrary units, often normalized by sample thickness, incident flux, and concentration to yield cross-sections in cm⁻¹ or absolute scale via standards like water. This framework, originating from early theoretical developments, provides the basis for interpreting SAXS patterns in terms of nanoscale density fluctuations.^[16]

Key Approximations and Laws

The Guinier approximation provides a fundamental tool for analyzing small-angle X-ray scattering (SAXS) data from dilute, monodisperse systems, enabling the determination of the radius of gyration R_g, a measure of particle size and shape. Derived from the low-q expansion of the scattering form factor P(q) using a Taylor series, it assumes spherical symmetry and negligible interparticle interactions, yielding the intensity expression

I(q) \approx I(0) \exp\left(-\frac{q^2 R_g^2}{3}\right),

where I(0) is the forward scattering intensity proportional to the particle's molecular weight and contrast, and q is the scattering vector. This approximation linearizes as \ln I(q) \approx \ln I(0) - \frac{q^2 R_g^2}{3} when plotted against q^2, allowing R_g to be extracted from the slope in the Guinier region.^[5] Porod's law describes the high-q regime of SAXS patterns for systems with sharp interfaces between phases of differing electron density, such as particles in solution, where surface scattering dominates over internal structure. For three-dimensional objects with smooth boundaries, the scattered intensity decays as I(q) \propto q^{-4}, reflecting the two-dimensional nature of the interface projected in reciprocal space. This power-law behavior arises from the Fourier transform of abrupt density changes, and the Porod invariant Q = 2\pi^2 \int_0^\infty q^2 I(q) \, dq integrates the full pattern to yield a value proportional to the volume fraction of scatterers and the squared electron density contrast (\Delta \rho)^2. The specific surface area S/V is given by S/V = \frac{1}{2\pi (\Delta \rho)^2} \lim_{q \to \infty} q^4 I(q), where the limit provides the Porod constant, providing quantitative insight into interfacial properties.^[18] The Kratky plot transforms SAXS data into q^2 I(q) versus q to assess the compactness and flexibility of macromolecules, particularly proteins, without assuming a specific model. For globular, folded structures, the plot exhibits a bell-shaped curve with a maximum around q R_g \approx 1.73 and decays to zero at high q, indicating a well-defined volume. In contrast, unfolded or intrinsically disordered proteins show a plateau at high q due to persistent chain flexibility, as the q^{-2} decay from random coil statistics combines with the q^2 multiplier to yield constant intensity. This representation highlights structural transitions, such as folding upon ligand binding, and is especially diagnostic for biological systems where hydration effects influence the apparent flexibility. In SAXS experiments, the scattering geometry influences data dimensionality: slit collimation, as in traditional Kratky cameras, integrates over a line source to produce inherently one-dimensional (1D) profiles with slit-length smearing that broadens peaks and requires desmearing corrections for accurate analysis. Pinhole collimation, common in modern synchrotron setups with two-dimensional (2D) detectors, captures azimuthal intensity distributions that are radially averaged to 1D curves, preserving higher resolution but demanding careful masking of beamstop shadows and parasitic scattering. The choice affects the accessible q-range and anisotropy detection, with 2D data enabling orientation studies in aligned samples. These approximations have specific validity ranges and assumptions that limit their application. The Guinier regime requires q R_g < 1 to avoid higher-order terms in the expansion, typically covering 0.1–1 nm⁻¹ for macromolecules up to 100 kDa, and assumes low concentrations (<1 mg/mL) to minimize forward scattering distortions from interactions. Porod's law holds for q > 1/R, where internal interferences fade, but breaks down for diffuse interfaces or polydispersity, leading to exponents between -3 and -4. The Kratky plot's qualitative insights depend on monodispersity and solvent matching, as aggregation or high contrast can mimic flexibility. Overall, these methods presuppose isotropic, dilute samples free of radiation damage, with deviations signaling the need for advanced modeling.^[2]

Experimental Methods

Instrumentation Components

Small-angle X-ray scattering (SAXS) experiments require specialized instrumentation to generate, shape, and detect X-rays at low scattering angles while minimizing background noise. The core hardware components include X-ray sources, monochromators and optics, collimation systems, sample environments, detectors, and vacuum paths. X-ray sources provide the incident beam, with choices depending on flux, energy tunability, and time resolution needs. Laboratory sources, such as rotating anode generators or microfocus sealed tubes, deliver moderate flux (typically 10^8–10^10 photons/s) suitable for static measurements of concentrated samples, operating at fixed energies around 8–12 keV.^[19] Synchrotron sources, like those at the ESRF or APS, offer orders-of-magnitude higher flux (up to 10^12–10^13 photons/s) and tunable energies (typically 8–20 keV), enabling studies of dilute solutions, time-resolved dynamics, and anomalous scattering.^[20] Emerging X-ray free-electron lasers (XFELs), such as LCLS or European XFEL, provide ultrafast pulses (femtoseconds) with peak brightness exceeding 10^32 photons/s/mm²/mrad²/0.1% BW, ideal for capturing non-equilibrium dynamics in biological and materials systems.^[21] Monochromators and optics select and focus the X-ray wavelength, typically 1–1.5 Å (12.4–8.3 keV), to ensure monochromaticity (Δλ/λ < 0.01) and beam quality. Double-crystal monochromators, often using Si(111) or Ge(111) reflections, provide high energy resolution and are standard at synchrotrons for clean beam selection.^[22] Multilayer optics, composed of alternating thin films (e.g., W/Si), offer broader bandwidth and higher throughput for laboratory or high-flux applications, though with slightly reduced resolution.^[23] Focusing elements, such as bent mirrors or toroidal optics, maintain beam divergence below 0.1 mrad to preserve angular resolution. Collimation systems define the beam geometry to achieve low divergence (<0.1 mrad) essential for small-angle resolution down to q ≈ 0.001 Å⁻¹. Point-collimation setups using pinhole apertures (50–500 µm diameter) or Kirkpatrick-Baez (KB) mirrors produce a focused 2D beam profile, enabling isotropic azimuthal averaging and studies of anisotropic samples.^[24] Line-collimation with slit systems or Göbel mirrors generates a 1D line focus for faster acquisition of radial profiles, commonly used in laboratory instruments for high-throughput screening.^[25] Sample environments accommodate diverse materials under controlled conditions. For solution-based SAXS, quartz or borosilicate capillaries (1–2 mm diameter) hold 10–50 µL volumes, minimizing beam absorption and enabling flow or static measurements. Solid or thin-film samples use specialized cells, such as diamond anvil or piston-cylinder setups, for in situ studies under temperature (up to 1500°C) and pressure (up to 0.7 GPa) variations to probe phase transitions.^[26] Detectors capture the scattered intensity with high spatial resolution and dynamic range to handle weak signals over 10^4–10^6 contrast ratios. 2D charge-coupled device (CCD) detectors, with pixel sizes of 20–50 µm, provide integrating readout for broad q-ranges but suffer from readout noise.^[27] Hybrid pixel array detectors, like the Pilatus series, employ photon-counting mode with 172 µm pixels, offering noise-free detection, 20-bit dynamic range, and frame rates up to 100 Hz for time-resolved SAXS. Vacuum paths, typically 1–30 m long flight tubes evacuated to <10⁻³ mbar, separate the sample from air to suppress parasitic scattering, which can obscure low-q signals by up to 50-fold compared to helium-filled alternatives.^[19] These paths, often with beamstops and guards, ensure clean data collection at synchrotron beamlines.^[28]

Measurement Procedures

Sample preparation is a critical step in SAXS experiments to obtain reliable scattering data free from artifacts such as aggregation or radiation-induced changes. For biological macromolecules like proteins, samples are typically prepared as aqueous solutions at concentrations of 1–10 mg/mL, which balances signal intensity with minimal inter-particle interference.^[29] To prevent oxidative damage during exposure, reducing agents such as 5–10 mM dithiothreitol (DTT) or 1–2 mM tris(2-carboxyethyl)phosphine (TCEP) are commonly added, while buffers are matched via multi-stage dialysis (16–48 hours) using membranes with molecular weight cut-off below the macromolecule mass.^[29] Samples must be degassed, centrifuged (e.g., at 10,000–20,000 g for 10–30 minutes), or filtered (0.22 μm pores) to eliminate aggregates or bubbles, ensuring monodispersity confirmed by preliminary checks like dynamic light scattering.^[30] Calibration standards, such as silver behenate, are prepared as thin films or powders for q-scale verification, with its lamellar structure providing a first Bragg peak at q = 0.1076 Å⁻¹ (d-spacing 58.38 Å). Beam alignment and calibration precede data acquisition to ensure accurate q-range coverage, typically from 0.006 to 1 Å⁻¹ for structural studies. Alignment involves centering the sample relative to the monochromatic X-ray beam (often 8–12 keV at synchrotrons) using fluorescent screens or ion chambers, with low vacuum or helium paths to reduce air scattering. The q-scale is determined by measuring the silver behenate standard, whose multiple diffraction rings allow precise angular calibration across low angles. Exposure times vary from 0.1–10 seconds per frame at high-flux synchrotron sources to 1–30 minutes in laboratory setups, optimized based on sample concentration and beam intensity to achieve sufficient statistics without damage.^[30] Multiple sample-to-detector distances (e.g., 0.3–4 m) may be used to extend the q-range, with data merged post-collection. Data collection modes are selected based on the scientific question, ranging from equilibrium to dynamic studies. In static mode, single-frame exposures capture time-averaged structures of stable samples, ideal for size and shape determination.^[29] Time-resolved SAXS employs rapid mixing devices, such as stopped-flow systems with dead times of 1–5 ms, to monitor kinetic processes like protein folding or assembly, often using flow cells (50–200 μL volume) for continuous or pump-probe setups.^[31] Anomalous SAXS achieves element-specific contrast variation by tuning the beam energy near the absorption edge (e.g., 7–10 keV for sulfur or iron), enabling selective probing of labeled sites in multicomponent systems like metalloprotein complexes.^[32] Background subtraction corrects for non-sample contributions to the scattering profile. Solvent or buffer scattering is measured separately under identical conditions and subtracted after scaling by the transmission factor (e.g., α ≈ 1 – c × 7.4 × 10⁻⁴ for proteins, where c is concentration in mg/mL).^[29] Empty cell measurements account for capillary or window contributions, while parasitic scattering from beam-defining slits or upstream components is masked or subtracted using geometric modeling. Artifacts and corrections address instrumental limitations during acquisition. A beam stop, typically a 1–3 mm diameter disk of tungsten or iridium, blocks the intense direct beam to prevent detector saturation and damage, creating a central data void filled by extrapolation. In slit-collimated geometries, such as Kratky cameras, azimuthal smearing broadens peaks and requires desmearing algorithms (e.g., Lake correction) to recover true point-collimation profiles. Safety protocols and throughput considerations are paramount, especially at synchrotron facilities. Radiation exposure is limited to avoid sample damage, with strategies including beam attenuation, sample translation or flow (1–10 μL/s), and exposures below 10¹¹–10¹² photons/s, monitored via radial averaging for intensity decay.^[33] Personal protective equipment and interlocks ensure operator safety from high-energy X-rays. Beamline scheduling allocates 8–48 hour shifts, enabling high throughput (10–100 samples/day) via automated sample changers, though demand often requires competitive proposals.^[30]

Data Analysis

Processing Techniques

The processing of raw small-angle X-ray scattering (SAXS) data begins with the conversion of two-dimensional detector images into one-dimensional scattering profiles, typically expressed as intensity I(q) versus the scattering vector q, where q = (4π/λ) sin(θ) and θ is half the scattering angle.^[34] This step is essential for isotropic samples, where the scattering is rotationally symmetric, enabling radial averaging to integrate pixel intensities over annular rings centered on the beam position.^[35] Accurate determination of the beam center, often using silver behenate standards, is critical for this integration to avoid distortions in the low-q region.^[35] For oriented samples exhibiting azimuthal anisotropy, sector integration is employed instead, averaging over specific angular sectors to preserve directional information.^[34] Normalization to absolute intensity scales the measured scattering cross-section to physical units, such as cm⁻¹, facilitating quantitative comparisons across experiments and samples. A common approach uses water as a secondary standard, where the forward scattering intensity I(0) of pure water at 20°C is theoretically known (approximately 0.0163 cm⁻¹), allowing calibration via transmission measurements of the sample and standard.^[36] Alternatively, glassy carbon standards provide a stable reference with certified scattering properties, particularly useful for beamline setups where water's temperature sensitivity is a concern. Transmission is typically measured using an ion chamber or photodiode to account for beam attenuation by the sample.^[35] Buffer subtraction removes the solvent contribution to isolate the particle scattering signal, requiring a matching buffer measurement under identical conditions to minimize mismatches in composition or temperature.^[29] The subtraction is performed by scaling the buffer profile to the sample's solvent region (high-q) and subtracting it from the total scattering, often followed by concentration normalization to express I(q) per unit mass or molar concentration for comparability.^[37] This step is crucial for dilute solutions, where buffer scattering can dominate at low q, and mismatches can introduce artifacts in structural parameters.^[37] Desmearing corrects for instrumental broadening due to finite slit or pinhole geometries, which smear the true point-collimated profile. The Lake method, an iterative algorithm, deconvolves the smearing function by assuming the true intensity is positive and monotonically decreasing, starting from an initial guess and refining until convergence. This technique, originally developed for slit-smeared data, has been adapted for modern pinhole cameras and is effective for q-ranges up to 0.5 Å⁻¹, though it requires careful regularization to avoid oscillations. Error estimation in processed SAXS profiles primarily relies on Poisson statistics for photon-counting detectors, where the variance in each pixel is equal to the number of counts, propagating through averaging and corrections as the square root of the summed intensities.^[38] Additional uncertainties arise from beam fluctuations, transmission measurements, and subtraction scaling, often modeled as a combination of Poisson noise and a flat systematic error (e.g., 5% of I(q)).^[38] These errors are propagated analytically or via Monte Carlo simulations to yield standard deviations for the final I(q) curve, ensuring reliable downstream analysis.^[34] Several software packages facilitate these processing steps, with the ATSAS suite providing tools for comprehensive analysis of biological SAXS data, including PRIMUS for normalization, subtraction, and error handling.^[39] Within ATSAS, GNOM performs desmearing alongside indirect Fourier transforms, though its primary role here is in preparatory corrections.^[40] BioXTAS RAW offers an open-source, user-friendly interface for radial averaging, buffer subtraction, and quick normalization, supporting formats from various beamlines and enabling batch processing for high-throughput experiments.

Modeling and Interpretation

Modeling and interpretation of small-angle X-ray scattering (SAXS) data involve computational methods to derive structural parameters from processed intensity profiles I(q) versus scattering vector q. Forward modeling typically employs least-squares fitting of parametric forms, such as spheres, cylinders, or ellipsoids, to the experimental data, allowing estimation of size, shape, and orientation parameters for rigid particles.^[41] Hybrid approaches integrate these fits with molecular dynamics (MD) simulations to refine models by comparing simulated scattering curves to measurements, enhancing accuracy for complex assemblies.^[42] Ab initio methods reconstruct low-resolution three-dimensional envelopes without prior structural assumptions, using dummy atom or residue representations packed into a search volume consistent with the data. Programs like DAMMIN employ simulated annealing to optimize bead positions that minimize discrepancies between calculated and experimental scattering, producing compact models suitable for globular proteins. For multi-component systems, MONSA extends this to multi-phase dummy atom modeling, simultaneously fitting multiple datasets (e.g., from X-ray and neutron scattering) to delineate distinct regions with different scattering lengths. The indirect Fourier transform provides a real-space representation by deconvolving the pair distance distribution function p(r) from I(q), revealing the maximum intramolecular dimension D_max and overall shape. Tools such as GNOM implement regularization to stabilize the ill-posed inversion, iteratively adjusting D_max to achieve a smooth p(r) that terminates near zero and fits the data well. This step aids in assessing particle dimensions and validating subsequent models. For flexible systems, ensemble modeling captures conformational variability by selecting subsets of conformations from a large pool that, when averaged, match the experimental SAXS profile. The Ensemble Optimization Method (EOM) within the ATSAS suite generates diverse linker and domain configurations via rapid coarse-grained modeling, then uses genetic algorithms to optimize sub-ensemble fractions for multi-state fits. This approach accounts for dynamic averaging inherent in solution scattering, distinguishing it from single-structure representations. Recent advances as of 2025 include tools like SAXS-A-FOLD, which optimize fits of AlphaFold-predicted structures with flexible regions to SAXS data, and SAXS Assistant, a Python-based script for automated feature extraction using machine learning.^[43]^[44] Model validation relies on quantitative metrics like the reduced chi-squared (\chi^2) value, which measures the goodness-of-fit between experimental and theoretical I(q) curves, ideally approaching 1 for unbiased models.^[45] Complementary techniques, such as nuclear magnetic resonance (NMR), provide orthogonal constraints; for instance, SAXS envelopes can validate NMR-derived structures by checking consistency in radius of gyration or overall shape. Advanced techniques incorporate Bayesian frameworks to quantify uncertainties in parameter estimates, treating models as probabilistic distributions and incorporating priors for physical realism during refinement against SAXS data. Machine learning methods enable pattern recognition in large datasets, such as classifying scattering profiles or automating model selection through supervised learning on feature vectors derived from I(q).

Applications

Biological Macromolecules

Small-angle X-ray scattering (SAXS) is widely employed to investigate the solution structures of biological macromolecules, including proteins, nucleic acids, and their complexes, providing insights into their size, shape, and assembly states under near-native conditions. Unlike high-resolution techniques such as X-ray crystallography, SAXS captures ensemble-averaged information from flexible or disordered systems in solution, making it particularly valuable for studying intrinsically disordered proteins (IDPs) and multi-domain architectures. Seminal work has demonstrated its utility in determining low-resolution envelopes that complement atomic models from other methods.^[46] In shape determination, SAXS yields key parameters such as the radius of gyration (R_g), which quantifies the overall size and compactness of macromolecules, and the maximum dimension (D_{\max}), which estimates the end-to-end distance from the pair distance distribution function p(r). For folded proteins like yeast pyruvate decarboxylase (PDC), R_g values around 2.5 nm indicate a compact globular form, while IDPs exhibit larger R_g (e.g., up to 4-5 nm for prothymosin α) reflecting extended conformations that compact under pH changes, such as a 10 Å reduction at low pH. These parameters distinguish folded from disordered states, with bell-shaped p(r) for globular proteins versus broader distributions for IDPs, enabling the characterization of conformational ensembles via methods like ensemble optimization modeling (EOM).^[10]^[47] Oligomerization and assembly processes are probed through the forward scattering intensity I(0), which scales with the square of the molecular weight, allowing detection of dimers, tetramers, or higher-order structures like viral capsids or fibrils. For instance, SAXS identified the tetrameric state of PDC (molecular weight ~240 kDa) and dimeric forms of αB-crystallin, while mixtures like telethonin-Z1Z2 complexes reveal equilibrium shifts via I(0) analysis. In assembly studies, SAXS tracks fibril formation in amyloidogenic proteins or capsid maturation in viruses by monitoring increases in I(0) and changes in R_g.^[10] Conformational changes induced by pH, temperature, or ligands are monitored by variations in scattering profiles, with time-resolved SAXS enabling kinetic studies of folding or transitions on timescales from milliseconds to seconds using synchrotron sources. Examples include the T-to-R allosteric transition in aspartate transcarbamylase (ATCase), occurring at rates of 0.05–3 s^{-1}, and temperature-induced compaction of the IDP Tau protein. Radiation damage is mitigated in these dynamic experiments through flow cells that continuously refresh the sample, ensuring data quality over multiple exposures.^[10]^[47] Contrast variation techniques in SAXS modulate electron density contrast using solvents or additives, such as sucrose solutions, glycerol, or iodinated contrast agents, to isolate contributions from specific components in complexes like multi-domain proteins or nucleoprotein assemblies. This approach highlights internal structures without isotopic labeling, complementing standard SAXS data. Hydration layer effects, which contribute to the scattering signal, are accounted for in modeling to avoid overestimation of particle size.^[10]^[48] SAXS integrates seamlessly with other structural biology methods, guiding rigid-body docking and refinement for complex assembly. Tools like pyDockSAXS use SAXS restraints to improve docking accuracy for protein-protein interactions, achieving higher success rates (up to 45% for challenging cases) by filtering decoy models against experimental profiles. In ribosome biogenesis, SAXS combined with crystallography modeled flexible proteins like ribosomal protein L12, revealing domain motions essential for function, while broader applications include hybrid modeling of multi-subunit complexes like the 30S ribosomal subunit.^[49]^[50] Challenges in biological SAXS include radiation damage from intense beams, which can alter protein structure; this is addressed using flow cells, cryoprotectants like glycerol, or attenuated fluxes to maintain monodispersity (>95%, verified by dynamic light scattering). Low signal-to-noise for dilute samples (~1-10 mg/mL) necessitates averaging multiple measurements, and hydration layer contributions must be modeled to interpret solvent-excluded volumes accurately. Despite these, SAXS remains indispensable for solution-phase studies of dynamic biomacromolecules.^[47]^[46]

Materials and Nanostructures

Small-angle X-ray scattering (SAXS) is widely employed to characterize the nanoscale structures in materials such as polymers, colloids, and nanomaterials, providing insights into particle size, shape, and distribution without requiring crystalline order. In nanoparticle systems, SAXS enables precise determination of core-shell architectures by analyzing the scattering intensity profiles, which reveal contrasts between the core and shell densities. For instance, in core-shell nanoparticles, the scattering data can be fitted to models that yield core radius, shell thickness, and polydispersity indices, typically on the order of 1-100 nm scales. This technique has been instrumental in studying gold nanoparticles coated with organic layers, where SAXS quantifies the "softness" of the coating through correlated scattering patterns. Porod analysis in SAXS is particularly valuable for assessing pore sizes and specific surface areas in mesoporous materials, where the high-q region of the scattering curve follows Porod's law, I(q) \propto q^{-4} for smooth interfaces, allowing extraction of interfacial area per unit volume via the Porod invariant Q = \int_0^\infty q^2 I(q) \, dq. Deviations from this exponent, such as a slope of -3.5 to -4, indicate rough or fractal interfaces in materials like silica-based mesopores. In model mesoporous silicas with cylindrical or spherical pores, SAXS combined with Porod fitting has validated pore diameters around 2-10 nm and surface areas exceeding 500 m²/g. For colloidal systems, SAXS monitors crystallization processes by tracking peak positions in scattering patterns, revealing lattice parameters and phase transitions in ordered assemblies.^[51]^[52]^[53] In block copolymers, SAXS elucidates microphase separation, where domain spacings of 10-100 nm form ordered structures like lamellae or cylinders, as evidenced by characteristic Bragg peaks in the scattering profile. Seminal studies on diblock copolymers have used synchrotron SAXS to observe the order-disorder transition, with domain sizes scaling with molecular weight according to theoretical predictions. Fractal dimensions in such materials are derived from power-law exponents in the intermediate q-range; for mass fractals, the scattering follows I(q) \propto q^{-D_m} where D_m < 3, quantifying self-similar clustering in polymer networks. Specific surface area from Porod invariant further aids in evaluating porosity in these phases.^[54]^[55]^[56] Grazing-incidence SAXS (GISAXS) extends these capabilities to thin films and interfaces, probing surface nanostructures with enhanced sensitivity to in-plane ordering, such as nanoparticle arrays on substrates, though limited here to standard SAXS contexts. In situ SAXS during polymer processing captures dynamic structural evolution, like chain alignment under shear, while in battery electrodes, it tracks electrode morphology changes, such as nanoparticle aggregation or pore evolution during charge-discharge cycles, revealing dimension shifts from 10 nm to microns. For carbon nanotubes, SAXS assesses alignment in forests or yarns, with azimuthal intensity distributions indicating orientation degrees up to 90% parallelism. In drug delivery, SAXS characterizes lipid bilayers in liposomes, determining bilayer thickness (around 4-5 nm) and drug incorporation effects on curvature, aiding optimization of encapsulation efficiency.^[57]^[58]^[59]

Advanced Variants

Resonant small-angle X-ray scattering (RASXS) enhances contrast in SAXS experiments by tuning the X-ray energy near the absorption edges of specific elements, enabling element-specific structural information without labeling. This technique exploits the anomalous dispersion of the atomic scattering factor to selectively highlight contributions from particular atomic species, such as transition metals in complex materials. In applications to magnetic nanostructures, RASXS has been used to probe the spatial distribution and magnetic ordering in thin films, revealing domain structures at the nanoscale through resonant enhancement of magnetic scattering signals. For instance, two-dimensional resonant magnetic soft X-ray scattering setups have demonstrated the ability to map magnetic correlations in cobalt-based multilayers with sub-10 nm resolution.^[60] Anomalous small-angle X-ray scattering (ASAXS) builds on this principle by systematically varying the X-ray energy across the absorption edge to decompose the total scattering intensity into contributions from different chemical components within a multicomponent sample. This energy-dependent approach allows separation of scattering from specific scatterers, such as distinguishing polymer phases or nanoparticles in blends based on their elemental composition. ASAXS is particularly valuable for studying phase separation and correlations in soft matter, where it provides chemical selectivity to the nanometer-scale morphology without requiring isotopic substitution. Seminal work has applied ASAXS to ionomers and block copolymers, quantifying the distribution of ions or specific blocks with high precision. In materials chemistry, ASAXS has elucidated the evolution of nanostructures during synthesis, such as in battery electrodes, by isolating scattering from metal atoms.^[61]^[62]^[63] Combined small- and wide-angle X-ray scattering (SAXS/WAXS) enables simultaneous probing of multi-scale structures, spanning from 1 nm to 100 nm in SAXS and down to atomic scales in WAXS, providing a comprehensive view of hierarchical materials in a single experiment. This integration captures both nanoscale morphology and local crystallinity or atomic packing, crucial for understanding processes like crystallization or phase transitions. Early implementations of combined setups have observed concurrent changes across nano- to micrometer ranges during inorganic solid crystallization, revealing nucleation and growth mechanisms in porous materials. Recent operando studies have utilized scanning SAXS/WAXS to track dynamic transformations in energy storage systems, such as lithium-sulfur batteries, over five orders of magnitude in momentum transfer.^[64] Grazing-incidence small-angle X-ray scattering (GISAXS) adapts the transmission SAXS geometry to reflection mode, allowing non-destructive analysis of surfaces, thin films, and buried interfaces with enhanced surface sensitivity. By directing the X-ray beam at a shallow grazing angle, GISAXS probes lateral nanostructures while minimizing penetration depth, ideal for studying film morphology, nanoparticle arrangements, and dewetting patterns in supported layers. The technique was pioneered for discontinuous thin films, where it distinguishes between island growth and coalescence through Yoneda peak analysis and distorted-wave Born approximation modeling. GISAXS has become essential for in situ monitoring of organic and inorganic thin film deposition, providing real-time insights into self-assembly on substrates.^[65] BioSAXS implementations emphasize high-throughput capabilities at synchrotron beamlines optimized for biological samples in solution, such as the ESRF BM29 beamline, which features automated sample changers for rapid data collection on proteins and complexes. These setups support unattended screening of hundreds of samples per shift, integrating online data processing for immediate quality assessment and structural parameter extraction. At the APS 12-ID-B beamline, simultaneous SAXS/WAXS modes facilitate high-flux measurements on dilute biomolecular solutions, enabling studies of conformational dynamics under physiological conditions. Such facilities have accelerated structural biology workflows, supporting ensemble modeling of flexible macromolecules.^[66]^[67]^[68] Emerging variants include serial femtosecond SAXS at X-ray free-electron lasers (XFELs), which captures ultrafast dynamics in non-crystalline samples using single-pulse diffraction before sample damage, ideal for time-resolved studies of biomolecular motions. This approach has determined molecular form factors from solution scattering patterns of proteins, enabling ab initio reconstruction of low-resolution envelopes without crystals. Polarized SAXS further probes anisotropy by exploiting the orientation dependence of scattering with linearly polarized beams, quantifying molecular alignment in oriented samples like polymer nanocomposites. Polarized resonant soft X-ray scattering variants have measured chain orientation in grafted nanoparticles, revealing local anisotropy through dichroic contrast.^[69]^[70]

References

[1]
Small-angle scattering for beginners - PMC - PubMed Central
Presented here is a rigorous discussion of small-angle scattering, at a technical level comparable to the classical undergraduate coverage of X-ray diffraction ...
[2]
Review of the fundamental theories behind small angle X-ray ... - NIH
This review presents several applications that highlight the ability of both SAXS and MD to study protein folding and function in addition to non-biological ...
[3]
Beyond simple small-angle X-ray scattering: developments in ... - NIH
When hard X-ray synchrotron radiation first became available, time-resolved SAXS was one of the techniques that attracted several pioneers. The earliest SAXS ...
[4]
Small Angle Scattering: Historical Perspective and Future Outlook
Small angle scattering (SAS) is a tool to elucidate the structure of matter at the nanometer scale, used in structural molecular biology.
[5]
[PDF] Introduction to Small-Angle X-ray Scattering - Stanford University
In small angle scattering the slight angle dependence (the so-called polarization factor) in the Thomson formula can be neglected. Page 5. Interference of waves.
[6]
A practical guide to small angle X-ray scattering (SAXS) of flexible ...
Sep 14, 2015 · Small-angle X-ray scattering (SAXS) is a biophysical method to study the overall shape and structural transitions of biological macromolecules in solution.
[7]
Growing a thriving international community for small-angle ... - NIH
In 1939, André Guinier published his landmark paper (Guinier, 1939 ▸) describing a simple approximate mathematical relationship between the rate of decrease in ...
[8]
Small-Angle X-ray Scattering for Pharmaceutical Applications
The author describes the development of small-angle X-ray scattering and analyzes its advantages in the characterization of drug-delivery systems and large ...
[9]
[PDF] Small-angle scattering studies of biological macromolecules in ...
Sep 16, 2003 · A breakthrough in SAXS and SANS experiments came in the 1970s, thanks to the availability of synchrotron radiation. (SR) and neutron sources, ...
[10]
(PDF) SAXS Instrumentation for Synchrotron Radiation then and now
Aug 10, 2025 · With advancements to brightness and stability in synchrotron radiation that began in the 1970s, SAXS was developed and refined at synchrotron ...
[11]
Integrative structural modeling with small angle X-ray scattering ...
Jul 16, 2012 · Here, we review specifically the use of SAXS profiles for the structural modeling of proteins, nucleic acids, and their complexes. First, the ...
[12]
Time-Resolved SAXS Screen of Small-Molecule Drug Candidates
Jun 24, 2024 · Time-resolved, high-throughput, small-angle x-ray scattering (SAXS) at the Advanced Light Source (ALS) improved the screening of small-molecule drug candidates.Missing: XFEL 2020-2025<|control11|><|separator|>
[13]
Microsecond time-resolved X-ray scattering by utilizing MHz ... - Nature
Jul 5, 2024 · Our new implementation of TR-WAXS realizes the unused potential of MHz XFELs to provide unique structural information about transient states on ...
[14]
https://als.lbl.gov/time-resolved-saxs-screen-of-small-molecule-drug-candidates/
[15]
Review of the fundamental theories behind small angle X-ray ...
In this paper, the fundamental concepts and equations necessary for performing small angle X-ray scattering (SAXS) experiments, molecular dynamics (MD) ...
[16]
https://doi.org/10.1107/S1600576721010293
[17]
small angle X-ray scattering – a critical review - IUCr Journals
This allows for the measurement of a smaller q range specific to the ultra-small angle regime, while utilizing a wide-range SAXS instrument for scattering at.
[18]
Form factor determination of biological molecules with X-ray ... - NIH
Oct 18, 2023 · The use of free-electron laser (FEL) X-rays to collect SAXS form factors of proteins in solution is demonstrated. Introduction. X-rays delivered ...
[19]
https://journals.iucr.org/j/issues/2018/06/00/kk5152/kk5152.pdf
[20]
Performance of a double-multilayer monochromator at Beamline 2 ...
Aug 6, 2025 · We describe the performance of the double-multilayer monochromator that is installed at bending magnet beamline 2-BM at the Advanced Photon ...
[21]
Hardware Optics | Small Angle X-ray Scattering/Diffraction
Kirkpatrick-Baez (KB) focussing mirror module. The KB system is an optional focusing module that enables SAXS data collection with beam sizes on the order of ...Missing: collimation pinhole slits Göbel
[22]
X-ray and neutron scattering instruments
... SAXS instruments employ so-called Kirkpatrick–Baez (KB) mirrors. ... Improvement of SAXS measurements on Kratky slit systems by Göbel mirrors and imaging-plate ...
[23]
High-pressure small-angle X-ray scattering cell for biological ... - NIH
In many cases pressure alters the molecular shape. Small-angle X-ray scattering (SAXS) is a primary method to determine the shape and size of macromolecules.
[24]
Transforming X-ray detection with hybrid photon counting detectors
Apr 29, 2019 · CCD detectors were severely limited in their dynamic range and added substantial readout noise to each exposure. Image plates required readout ...Missing: 2D | Show results with:2D
[25]
Small Angle X-ray Scattering (SAXS) Diffractometer - UCSB MRL
Background scattering is minimized through the use of an evacuated flight path and vacuum compatible motorized slits. Designed and constructed by ...
[26]
Sample preparation, data collection and preliminary data analysis in ...
In rare cases when vacuum is not attainable, the tube should be filled with helium since its X-ray scatter is smaller by a factor of 50 than that of the air.Synchrotron Saxs Data... · Saxs Data Processing... · Saxs Data Analysis
[27]
Synchrotron-based small-angle X-ray scattering (SAXS) of proteins ...
Here, we present a series of procedures that can be used for SAXS data collection and basic cross-checks designed to detect and avoid aggregation, concentration ...Beamline Settings · Procedure · Anticipated Results
[28]
Structural Kinetics of MsbA Investigated by Stopped-Flow Time ...
Mar 3, 2020 · Time-resolved small-angle X-ray scattering using stopped-flow mixing to initiate the reaction (SF-TR-SAXS) is a powerful technique to monitor ...
[29]
Anomalous Small-Angle X-Ray Scattering (ASAXS) - SpringerLink
Anomalous small-angle scattering of X-rays (ASAXS) is a technique which allows one to obtain contrast variation in a multicomponent system.Missing: measurement procedures
[30]
[PDF] Limiting radiation damage for high-brilliance biological solution ...
Jan 8, 2015 · Strategies to reduce radiation damage include increased sample flow, translating the sample, beam attenuation, defocusing, reduced exposure, ...Missing: safety | Show results with:safety
[31]
small-angle scattering pattern collection and correction - IOPscience
This work is intended to provide a comprehensive overview of all data corrections, to aid the small-angle scatterer to decide which are relevant for their ...Missing: artifacts | Show results with:artifacts
[32]
[PDF] SAXS/SANS data processing and overall parameters
Radial integration of 2D image into 1D curve. • Exact coordinates of the beam center are required for integration (determined from AgBeh data).
[33]
Methods, development and applications of small-angle X-ray ... - NIH
Small-angle X-ray scattering (SAXS) is a powerful technique in structural biology. · SAXS allows to study biological macromolecules in close to native solutions.
[34]
Analysis of small-angle X-ray scattering data in the presence of ...
Dec 6, 2015 · The two-dimensional scattering patterns of the beam were radially averaged in the same way as the sample spectra. 3. Collimation smearing. 3.1.
[35]
Quantitative evaluation of statistical errors in small-angle X-ray ...
Mar 29, 2017 · A new model is proposed for the measurement errors incurred in typical small-angle X-ray scattering (SAXS) experiments, which takes into account the setup ...
[36]
ATSAS 2.8: a comprehensive data analysis suite for small-angle ...
ATSAS is a comprehensive software suite for the analysis of small-angle scattering data from dilute solutions of biological macromolecules or nanoparticles.
[37]
GNOM - Biological small angle scattering - EMBL Hamburg
Jul 7, 2014 · GNOM is an indirect transform program for small-angle scattering data processing. It reads in one-dimensional scattering curves.
[38]
[PDF] Analysis of small-angle scattering data from colloids and polymer ...
Analysis of small-angle scattering uses least-squares methods, including indirect Fourier transformation, square-root deconvolution, and size distribution ...
[39]
Data analysis software ATSAS - Biological small angle scattering
Sep 9, 2022 · A program suite for small-angle scattering data analysis from biological macromolecules. Experimental data processing.GNOM · Download ATSAS · Primus · Crysol
[40]
Small-Angle X-Ray Scattering on Biological Macromolecules and ...
Apr 1, 2013 · This review describes the analysis methods of SAXS data from macromolecular solutions, ranging from the computation of overall structural parameters to ...
[41]
A practical guide to small angle X‐ray scattering (SAXS) of flexible ...
Aug 29, 2015 · SAXS provides low resolution information on the shape, conformation and assembly state of proteins, nucleic acids and various macromolecular ...<|control11|><|separator|>
[42]
pyDockSAXS: protein–protein complex structure by SAXS and ... - NIH
Provides an automatic pipeline for modeling the structure of a protein–protein complex from SAXS data.Missing: review | Show results with:review
[43]
Structure and Dynamics of Ribosomal Protein L12 - NIH
The ensemble model reveals intrinsic conformational properties of L12 that help explain its function on the ribosome. The two C-terminal domains sample a large ...Material And Methods · Saxs Data Collection And... · Results<|control11|><|separator|>
[44]
SAXS analysis of mesoporous model materials: a validation of data ...
Two model mesoporous silicas with cylindrical and spherical mesopore architectures were analyzed with SAXS, using evaluation principles introduced by Ruland.
[45]
A negative deviation from Porod's law in SAXS of organo-MSU-X
In particular, SAXS can be used to study the interfacial characteristics between two phases according to a negative deviation of SAXS intensities from Porod's ...
[46]
[PDF] Small Angle X-ray Scattering analysis of porous powders of CaCO3
Mar 10, 2021 · In the SAXS analysis, we first apply the Guinier–Porod model and then we use the Porod invariant to extract the porosity and specific surface ...<|control11|><|separator|>
[47]
Synchrotron SAXS study of the microphase separation transition in ...
Synchrotron SAXS study of the microphase separation transition in diblock copolymers ... Morphological and Scattering Studies of Binary Mixtures of Block ...
[48]
(PDF) Theory of Microphase Separation in Block Copolymers
A microscopic statistical theory of phase equilibria in noncrystalline block copolymers of type AB is developed.
[49]
Small-Angle Scattering from Fractals: Differentiating between ... - MDPI
Exponents of power-law decays in each fractal region, A succession of mass-to-surface fractal generalized power-law decays, with exponents D m , and ...
[50]
In Situ SAXS Studies of the Structural Changes of Polymer ...
Aug 10, 2025 · In situ small-angle X-ray scattering studies have been conducted to monitor the structural changes of polymer nanocomposites upon heating.
[51]
Small angle X-ray scattering study of carbon nanotube forests ...
Oct 1, 2013 · SAXS ... Here we present a systematic study on the analysis of the alignment of carbon nanotubes within solvent densified carbon nanotube forests.
[52]
Small Angle X-ray and Neutron Scattering: Powerful Tools for ... - NIH
Mar 28, 2016 · SAXS makes it possible to reconstruct the structure of drug carriers alone or loaded with drugs in a natural aqueous environment [22]. The ...
[53]
[PDF] Two-dimensional resonant magnetic soft X-ray scattering ... - Hal-CEA
Jan 23, 2017 · The MagSAXS (magnetic small-angle X-ray scattering) set- up presented here consists of a reflection geometry under critical or sub-critical ...Missing: RASXS | Show results with:RASXS
[54]
Anomalous small-angle X-ray scattering: analyzing correlations and ...
We review recent structural investigations done by anomalous small-angle X-ray scattering (ASAXS). ASAXS uses the dependence of the scattering length of a ...Missing: seminal | Show results with:seminal
[55]
Anomalous small-angle X-ray scattering for materials chemistry
In situ small-angle X-ray scattering (SAXS) represents one of the techniques for studying the evolution kinetics of materials structures.Missing: seminal paper
[56]
Anomalous Small-Angle X-ray Scattering and Its Application in the ...
Anomalous small-angle X-ray scattering (ASAXS) is one of the most effective techniques for studying nanostructural change in an operando way.
[57]
Multiscale operando X-ray investigations provide insights into ...
Oct 1, 2021 · The combination of USAXS + SAXS + WAXS achieved a five-decades combined Q-range in scatter sizes from 10−4/Å to 6.6/Å, corresponding to a ...
[58]
Grazing‐incidence small‐angle X‐ray scattering: new tool for ...
GISAXS studies discontinuous thin films by reflecting a beam from the substrate, then scattering the refracted beam by the film. It is non-destructive and can ...
[59]
BM29 BioSAXS - European Synchrotron Radiation Facility (ESRF)
The BioSAXS beamline is a highly automated beamline dedicated to the study of proteins, macromolecular complexes, viruses etc., in solution.Missing: ID14 APS ID- B
[60]
Upgraded ESRF BM29 beamline for SAXS on macromolecules in ...
BM29 is a fully automated high-throughput beamline dedicated to proteins in solution which facilitates experiments for researchers. Similar high-throughput SAXS ...
[61]
12-ID-B Home Page | Advanced Photon Source
Apr 4, 2022 · Beamline 12-ID-B is a dedicated X-ray scattering beamline at APS. It routinely runs simutanous small- and wide-angle X-ray scattering (SAXS ...Missing: ESRF | Show results with:ESRF
[62]
Form factor determination of biological molecules with X-ray free ...
Oct 18, 2023 · SAXS allows the study of the shape and overall structure of proteins and nucleic acids in solution, in a quasi-native environment. In solution, ...
[63]
Polarized X-ray scattering measures molecular orientation ... - Nature
Aug 12, 2021 · Here, we directly measure local chain orientation in polystyrene grafted gold nanoparticles using polarized resonant soft X-ray scattering (P-RSoXS).