Fitting low-resolution cryo-EM maps of proteins using constrained geometric simulations.

ABSTRACT: Recent experimental advances in producing density maps from cryo-electron microscopy (cryo-EM) have challenged theorists to develop improved techniques to provide structural models that are consistent with the data and that preserve all the local stereochemistry associated with the biomolecule. We develop a new technique that maintains the local geometry and chemistry at each stage of the fitting procedure. A geometric simulation is used to drive the structure from some appropriate starting point (a nearby experimental structure or a modeled structure) toward the experimental density, via a set of small incremental motions. Structural motifs such as alpha-helices can be held rigid during the fitting procedure as the starting structure is brought into alignment with the experimental density

SUBMITTER: Jolley CC 

PROVIDER: S-EPMC2242741 | biostudies-literature | 2008 Mar

REPOSITORIES: biostudies-literature