Atomic-accuracy models from 4.5-Å cryo-electron microscopy data with density-guided iterative local refinement

Frank DiMaio

doi:10.1038/NMETH.3286

Atomic-accuracy models from 4.5-Å cryo-electron microscopy data with density-guided iterative local refinement

2015-02-23

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Vincent P. Conticello

DOI：10.1038/NMETH.3286

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We describe a general approach for refining protein structure models on the basis of cryo-electron microscopy maps with near-atomic resolution. The method integrates Monte Carlo sampling with local density-guided optimization, Rosetta all-atom refinement and real-space B-factor fitting. In tests on experimental maps of three different systems with 4.5-angstrom resolution or better, the method consistently produced models with atomic-level accuracy largely independently of starting-model quality, and it outperformed the molecular dynamics-based MDFF method. Cross-validated model quality statistics correlated with model accuracy over the three test systems.

Keywords:

PROTEIN STRUCTURES

STRUCTURE VALIDATION

ELECTRON

MOLPROBITY

PHENIX

SPACE

Atomic-accuracy models from 4.5-Å cryo-electron microscopy data with density-guided iterative local refinement

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