Building and refining protein models within cryo-electron microscopy density maps based on homology modeling and multiscale structure refinement.

ABSTRACT: Automatic modeling methods using cryoelectron microscopy (cryoEM) density maps as constraints are promising approaches to building atomic models of individual proteins or protein domains. However, their application to large macromolecular assemblies has not been possible largely due to computational limitations inherent to such unsupervised methods. Here we describe a new method, EM-IMO (electron microscopy-iterative modular optimization), for building, modifying and refining local structures of protein models using cryoEM maps as a constraint. As a supervised refinement method, EM-IMO allows users to specify parameters derived from inspections so as to guide, and as a consequence, significantly speed up the refinement. An EM-IMO-based refinement protocol is first benchmarked on a data set

SUBMITTER: Zhu J 

PROVIDER: S-EPMC2860449 | biostudies-literature | 2010 Apr

REPOSITORIES: biostudies-literature