TY - JOUR
T1 - FoXS, FoXSDock and MultiFoXS
T2 - Single-state and multi-state structural modeling of proteins and their complexes based on SAXS profiles
AU - Schneidman-Duhovny, Dina
AU - Hammel, Michal
AU - Tainer, John A.
AU - Sali, Andrej
N1 - Funding Information: SAXS at the Advanced Light Source SIBLYS beamline in supported by National Institutes of Health (NIH) grants CA92584 and MINOS GM105404, United States Department of Energy program IDAT, plus industrial partners Biogen and Janssen Pharmaceutica. This work was supported by grants from the NIH R01 GM083960 and NIH P41 GM109824. Conflict of interest statement. None declared. Publisher Copyright: © The Author(s) 2016.
PY - 2016
Y1 - 2016
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=85013011986&partnerID=8YFLogxK
U2 - https://doi.org/10.1093/nar/gkw389
DO - https://doi.org/10.1093/nar/gkw389
M3 - Article
C2 - 27151198
SN - 0305-1048
VL - 44
SP - W424-W429
JO - Nucleic acids research
JF - Nucleic acids research
IS - 1
ER -