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

We present a de novo model building approach that combines predicted backbone conformations with side-chain density-fit to accurately assign sequence into density maps. We show this method yields accurate models for six experimental maps at 3.3–4.8 Å resolution, and produces a nearly complete model...

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Detalles Bibliográficos
Autores principales: Wang, Ray Yu-Ruei, Kudryashev, Mikhail, Li, Xueming, Egelman, Edward H., Basler, Marek, Cheng, Yifan, Baker, David, DiMaio, Frank
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2015
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4435692/
https://www.ncbi.nlm.nih.gov/pubmed/25707029
http://dx.doi.org/10.1038/nmeth.3287
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author Wang, Ray Yu-Ruei
Kudryashev, Mikhail
Li, Xueming
Egelman, Edward H.
Basler, Marek
Cheng, Yifan
Baker, David
DiMaio, Frank
author_facet Wang, Ray Yu-Ruei
Kudryashev, Mikhail
Li, Xueming
Egelman, Edward H.
Basler, Marek
Cheng, Yifan
Baker, David
DiMaio, Frank
author_sort Wang, Ray Yu-Ruei
collection PubMed
description We present a de novo model building approach that combines predicted backbone conformations with side-chain density-fit to accurately assign sequence into density maps. We show this method yields accurate models for six experimental maps at 3.3–4.8 Å resolution, and produces a nearly complete model for an unsolved map containing a 660-residue hetero-dimeric protein. This method should enable rapid and reliable protein structure determination from near-atomic resolution cryo-EM maps.
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spelling pubmed-44356922015-10-01 De novo protein structure determination from near-atomic resolution cryo-EM maps Wang, Ray Yu-Ruei Kudryashev, Mikhail Li, Xueming Egelman, Edward H. Basler, Marek Cheng, Yifan Baker, David DiMaio, Frank Nat Methods Article We present a de novo model building approach that combines predicted backbone conformations with side-chain density-fit to accurately assign sequence into density maps. We show this method yields accurate models for six experimental maps at 3.3–4.8 Å resolution, and produces a nearly complete model for an unsolved map containing a 660-residue hetero-dimeric protein. This method should enable rapid and reliable protein structure determination from near-atomic resolution cryo-EM maps. 2015-02-23 2015-04 /pmc/articles/PMC4435692/ /pubmed/25707029 http://dx.doi.org/10.1038/nmeth.3287 Text en http://www.nature.com/authors/editorial_policies/license.html#terms Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Wang, Ray Yu-Ruei
Kudryashev, Mikhail
Li, Xueming
Egelman, Edward H.
Basler, Marek
Cheng, Yifan
Baker, David
DiMaio, Frank
De novo protein structure determination from near-atomic resolution cryo-EM maps
title De novo protein structure determination from near-atomic resolution cryo-EM maps
title_full De novo protein structure determination from near-atomic resolution cryo-EM maps
title_fullStr De novo protein structure determination from near-atomic resolution cryo-EM maps
title_full_unstemmed De novo protein structure determination from near-atomic resolution cryo-EM maps
title_short De novo protein structure determination from near-atomic resolution cryo-EM maps
title_sort de novo protein structure determination from near-atomic resolution cryo-em maps
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4435692/
https://www.ncbi.nlm.nih.gov/pubmed/25707029
http://dx.doi.org/10.1038/nmeth.3287
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