PRISM-EM: template interface-based modelling of multi-protein complexes guided by cryo-electron microscopy density maps.

ABSTRACT: The structures of protein assemblies are important for elucidating cellular processes at the molecular level. Three-dimensional electron microscopy (3DEM) is a powerful method to identify the structures of assemblies, especially those that are challenging to study by crystallography. Here, a new approach, PRISM-EM, is reported to computationally generate plausible structural models using a procedure that combines crystallographic structures and density maps obtained from 3DEM. The predictions are validated against seven available structurally different crystallographic complexes. The models display mean deviations in the backbone of <5 Å. PRISM-EM was further tested on different benchmark sets; the accuracy was evaluated with respect to the structure of the complex, and the correlation wit

SUBMITTER: Kuzu G 

PROVIDER: S-EPMC5053140 | biostudies-literature | 2016 Oct

REPOSITORIES: biostudies-literature