Automated real-space refinement of protein structures using a realistic backbone move set.

ABSTRACT: Crystals of many important biological macromolecules diffract to limited resolution, rendering accurate model building and refinement difficult and time-consuming. We present a torsional optimization protocol that is applicable to many such situations and combines Protein Data Bank-based torsional optimization with real-space refinement against the electron density derived from crystallography or cryo-electron microscopy. Our method converts moderate- to low-resolution structures at initial (e.g., backbone trace only) or late stages of refinement to structures with increased numbers of hydrogen bonds, improved crystallographic R-factors, and superior backbone geometry. This automated method is applicable to DNA-binding and membrane proteins of any size and will aid studies of structural bi

SUBMITTER: Haddadian EJ 

PROVIDER: S-EPMC3175057 | biostudies-literature | 2011 Aug

REPOSITORIES: biostudies-literature