Accurate optimization of amino acid form factors for computing small-angle X-ray scattering intensity of atomistic protein structures.

ABSTRACT: Structure modelling via small-angle X-ray scattering (SAXS) data generally requires intensive computations of scattering intensity from any given biomolecular structure, where the accurate evaluation of SAXS profiles using coarse-grained (CG) methods is vital to improve computational efficiency. To date, most CG SAXS computing methods have been based on a single-bead-per-residue approximation but have neglected structural correlations between amino acids. To improve the accuracy of scattering calculations, accurate CG form factors of amino acids are now derived using a rigorous optimization strategy, termed electron-density matching (EDM), to best fit electron-density distributions of protein structures. This EDM method is compared with and tested against other CG SAXS computing met

SUBMITTER: Tong D 

PROVIDER: S-EPMC5223287 | biostudies-literature | 2016 Aug

REPOSITORIES: biostudies-literature