The use of local structural similarity of distant homologues for crystallographic model building from a molecular-replacement solution.

ABSTRACT: The performance of automated protein model building usually decreases with resolution, mainly owing to the lower information content of the experimental data. This calls for a more elaborate use of the available structural information about macromolecules. Here, a new method is presented that uses structural homologues to improve the quality of protein models automatically constructed using ARP/wARP. The method uses local structural similarity between deposited models and the model being built, and results in longer main-chain fragments that in turn can be more reliably docked to the protein sequence. The application of the homology-based model extension method to the example of a CFA synthase at 2.7 Å resolution resulted in a more complete model with almost all of the residues correctly b

SUBMITTER: Chojnowski G 

PROVIDER: S-EPMC7057216 | biostudies-literature | 2020 Mar

REPOSITORIES: biostudies-literature