Marbles is novel software that employs SAXS intensities to predict the shape of membrane proteins embedded into membrane nanodiscs.

A method is described for determining the 3D structure of a sample from X-ray free-electron laser single-particle diffraction patterns by analyzing different orders of spatial correlations of diffraction intensities.

The influence of polychromaticity on SAXS data analysis is discussed. It is concluded that SAXS data collected in pink-beam mode can be used directly for structural calculations and model reconstructions without a desmearing procedure.

This article reports the integral transform that determines the particle size distribution from the small-angle scattering intensity under the assumption that the particle correlation function is a polynomial.

DAMMIF, an enhanced and significantly faster implementation of the ab-initio shape-determination program DAMMIN for small-angle scattering data, is presented.

The size and size anisotropy of nanocrystals is determined together with the distribution of amorphous phases inside a seven-capillary model reactor filled with various nanomaterials. This is achieved by diffraction scattering computed tomography followed by Rietveld refinement and multivariate analysis of Rietveld backgrounds.

The effects of bandwidth, spectral shape and high harmonics for undulator sources on SAXS measurements are evaluated quantitatively. Monodisperse and polydisperse systems are explored.

Reconstruction of an object from the averaged coherent diffracted intensity of finite crystals of that object with arbitrary lattice occupancies is possible. An algorithm capable of reconstructing both the so-called averaged shape transform and the object density at the same time is demonstrated.

A combined ab initio and rigid-body approach has been developed for small-angle scattering analysis. This provides a previously inaccessible insight into the low-resolution structure of the human cytochrome P450 CYP3A4 when embedded in nanodiscs mimicking a native membrane.

This paper discusses the execution of numerous simultaneous runs of the programs DAMMIN and GASBOR using Condor, which distributes them over a network of PCs; this has allowed a substantial acceleration of the processing of results. The application of Condor to determine the molecular shape of tissue transglut­aminase is presented, thus demonstrating the efficiency of the approach.