Fitmunk: improving protein structures by accurate, automatic modeling of side-chain conformations.

ABSTRACT: Improvements in crystallographic hardware and software have allowed automated structure-solution pipelines to approach a near-`one-click' experience for the initial determination of macromolecular structures. However, in many cases the resulting initial model requires a laborious, iterative process of refinement and validation. A new method has been developed for the automatic modeling of side-chain conformations that takes advantage of rotamer-prediction methods in a crystallographic context. The algorithm, which is based on deterministic dead-end elimination (DEE) theory, uses new dense conformer libraries and a hybrid energy function derived from experimental data and prior information about rotamer frequencies to find the optimal conformation of each side chain. In contrast to existing

SUBMITTER: Porebski PJ 

PROVIDER: S-EPMC4756610 | biostudies-literature | 2016 Feb

REPOSITORIES: biostudies-literature