Accurate SAXS profile computation and its assessment by contrast variation experiments.

ABSTRACT: A major challenge in structural biology is to characterize structures of proteins and their assemblies in solution. At low resolution, such a characterization may be achieved by small angle x-ray scattering (SAXS). Because SAXS analyses often require comparing profiles calculated from many atomic models against those determined by experiment, rapid and accurate profile computation from molecular structures is needed. We developed fast open-source x-ray scattering (FoXS) for profile computation. To match the experimental profile within the experimental noise, FoXS explicitly computes all interatomic distances and implicitly models the first hydration layer of the molecule. For assessing the accuracy of the modeled hydration layer, we performed contrast variation experiments for glucose isom

SUBMITTER: Schneidman-Duhovny D 

PROVIDER: S-EPMC3752106 | biostudies-literature | 2013 Aug

REPOSITORIES: biostudies-literature