Polarizable atomic multipole x-ray refinement: hydration geometry and application to macromolecules.

ABSTRACT: We recently developed a polarizable atomic multipole refinement method assisted by the AMOEBA force field for macromolecular crystallography. Compared to standard refinement procedures, the method uses a more rigorous treatment of x-ray scattering and electrostatics that can significantly improve the resultant information contained in an atomic model. We applied this method to high-resolution lysozyme and trypsin data sets, and validated its utility for precisely describing biomolecular electron density, as indicated by a 0.4-0.6% decrease in the R- and R(free)-values, and a corresponding decrease in the relative energy of 0.4-0.8 Kcal/mol/residue. The re-refinements illustrate the ability of force-field electrostatics to orient water networks and catalytically relevant hydrogens, which ca

SUBMITTER: Fenn TD 

PROVIDER: S-EPMC2884231 | biostudies-literature | 2010 Jun

REPOSITORIES: biostudies-literature