FoXS, FoXSDock and MultiFoXS: Single-state and multi-state structural modeling of proteins and their complexes based on SAXS profiles

By Dina Schneidman-Duhovny, M. Hammel, John A. Tainer, Andrej Sali. Nucleic Acids Res., 2016

458 citations recorded by the source corpus.

Small Angle X-ray Scattering (SAXS) is an increasingly common and useful technique for structural characterization of molecules in solution. A SAXS experiment determines the scattering intensity of a molecule as a function of spatial frequency, termed SAXS profile. Here, we describe three web servers for modeling atomic structures based on SAXS profiles. FoXS (Fast X-Ray Scattering) rapidly computes a SAXS profile of a given atomistic model and fits it to an experimental profile. FoXSDock docks two rigid protein structures based on a SAXS profile of their complex. MultiFoXS computes a population-weighted ensemble starting from a single input structure by fitting to a SAXS profile of the protein in solution. We describe the interfaces and capabilities of the servers (salilab.org/foxs), followed by demonstrating their application on Interleukin-33 (IL-33) and its primary receptor ST2.

Subfields: Immunology

View Paper: https://www.semanticscholar.org/paper/4ee93f0df1de328d454d0bf1de0a166378f24783

Citations in the corpus

• BioXTAS RAW: improvements to a free open-source program for small-angle X-ray scattering data reduction and analysis (2017, unknown): “…DENFERT, SASTBX, MEMPROT (Curtis et al., 2012; Liu et al., 2012; Koutsioubas & Pérez, 2013; Spinozzi et al., 2014; Pérez & Koutsioubas, 2015; Koutsioubas et al., 2016; Perkins et al., 2016; Schneidman-Duhovny et al., 2016) and more (see, for example, http://smallangle.org/content/software).”