Format

Send to

Choose Destination
Nat Methods. 2015 Apr;12(4):335-8. doi: 10.1038/nmeth.3287. Epub 2015 Feb 23.

De novo protein structure determination from near-atomic-resolution cryo-EM maps.

Author information

1
1] Graduate program in Biological Physics, Structure and Design, University of Washington, Seattle, Washington, USA. [2] Department of Biochemistry, University of Washington, Seattle, Washington, USA.
2
1] Focal Area Infection Biology, Biozentrum, University of Basel, Basel, Switzerland. [2] Center for Cellular Imaging and NanoAnalytics, Biozentrum, University of Basel, Basel, Switzerland.
3
The Keck Advanced Microscopy Laboratory, Department of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, California, USA.
4
Department of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, Virginia, USA.
5
Focal Area Infection Biology, Biozentrum, University of Basel, Basel, Switzerland.
6
1] Department of Biochemistry, University of Washington, Seattle, Washington, USA. [2] Howard Hughes Medical Institute, University of Washington, Seattle, Washington, USA.
7
Department of Biochemistry, University of Washington, Seattle, Washington, USA.

Abstract

We present a de novo model-building approach that combines predicted backbone conformations with side-chain fit to density to accurately assign sequence into density maps. This method yielded accurate models for six of nine experimental maps at 3.3- to 4.8-Å resolution and produced a nearly complete model for an unsolved map containing a 660-residue heterodimeric protein. This method should enable rapid and reliable protein structure determination from near-atomic-resolution cryo-electron microscopy (cryo-EM) maps.

PMID:
25707029
PMCID:
PMC4435692
DOI:
10.1038/nmeth.3287
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Nature Publishing Group Icon for PubMed Central
Loading ...
Support Center