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

A method is described for reconstructing the shapes of protein molecules from X-ray solution scattering data, which involves the progressive confinement of a set of interacting volume-defining points to fit the expected protein volume. Tests with synthetic and experimental data demonstrate that the final distributions of points obtained using this approach correctly map out the protein envelope.

Ambiguities in and the completeness of SAS data analysis of membrane proteins (MPs) are considered here in the case of the sensory rhodopsin II–transducer complex solubilized in a detergent. The contribution of the detergent belt surrounding MPs is one of the main problems in SAS data analysis of MPs; the second problem addressed here is the influence of oligomerization polydispersity (which is a sufficiently common phenomenon for MPs) on the quality of SAS structural analysis.

The development of instrumentation and software to support mail-in solution scattering is presented.

BioXTAS RAW is a graphical-user-interface-based free open-source Python program for reduction and analysis of small-angle X-ray solution scattering (SAXS) data, including size-exclusion chromatography coupled SAXS data. The software is designed for biological data and enables creation and plotting of one-dimensional scattering profiles from two-dimensional detector images, standard data operations such as averaging and subtraction and analysis of radius of gyration and molecular weight, and more advanced analyses such as calculation of inverse Fourier transforms.

A quantitative resolution measure of the ab initio shapes restored from small-angle scattering data is introduced based on the variability of multiple reconstructions. The new measure is validated in simulated examples and its efficiency has been demonstrated in applications to experimental data.

A method is presented to quantitatively assess the inherent ambiguity of three-dimensional shape reconstruction from a given small-angle scattering pattern.

The structural characterization of the N-terminal part of the nucleocapsid from Middle East respiratory syndrome coronavirus (MERS-CoV), a recently emerging virus, is reported. The structure of the N-terminal region, which includes a disordered tail followed by a globular domain, was obtained by combining X-ray diffraction and SAXS.

A method utilizing a spherical harmonics representation of the scattering amplitudes for a rapid superposition of three-dimensional models is developed.

The residues Lys271, Ser266 and Thr267 of the linker region that connects the methyltransferase and RNA-dependent RNA polymerase domains of dengue virus NS5 serotype 4 are important for differential compactness.