Evidence map›Paper›PMID 27669148›Full record

ArticleeLife2016

Automated structure refinement of macromolecular assemblies from cryo-EM maps using Rosetta.

Ray Yu-Ruei Wang, Yifan Song, Benjamin A Barad, Yifan Cheng, James S Fraser, Frank DiMaio

Abstract read
In one paragraph

Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 356 papers.

0numbers the graph read from it
0cells of the map it votes in
356citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

356 citing papers in PubMed.

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296 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors.

Ray Yu-Ruei WangGraduate Program in Biological Physics, Structure and Design, University of Washington, Seattle, United States.ORCID 0000-0001-5025-9596
Yifan SongDepartment of Biochemistry, University of Washington, Seattle, United States.
Benjamin A BaradDepartment of Bioengineering and Therapeutic Science, University of California, San Francisco, San Francisco, United States.ORCID 0000-0002-1016-862X
Yifan ChengKeck Advanced Microscopy Laboratory, University of California, San Francisco, San Francisco, United States.
James S FraserDepartment of Bioengineering and Therapeutic Science, University of California, San Francisco, San Francisco, United States.ORCID 0000-0002-5080-2859
Frank DiMaioDepartment of Biochemistry, University of Washington, Seattle, United States.ORCID 0000-0002-7524-8938

Funding

X-ray Screening and Rapid Structure DeterminationP50GM082250 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI KROGAN, NEVAN J · 2007 to 2018
$48.8M
STRUCTURAL BIOLOGY TRAINING PROGRAMT32GM008284 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI KORTEMME, TANJA · 1988 to 2022
$10.1M
Structure, States and Transition in ABC Transporters pp360-431P01GM111126 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI SALI, ANDREJ · 2015 to 2019
$9.8M
Integrative Program in Complex Biological System (ipCBS)T32EB009383 · NIBIB · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI MARSHALL, WALLACE, WEINER, ORION D · 2009 to 2022
$3.2M
Structures and gating mechanisms of TRP ion channelsR01GM098672 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI CHENG, YIFAN · 2011 to 2018
$2.6M
Model Comparison in Structural BiologyR21GM110580 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FRASER, JAMES SOLOMON · 2014 to 2015
$419k
NIBIB NIH HHS T32 EB009383NIGMS NIH HHS P01 GM111126NIGMS NIH HHS P50 GM082250NIGMS NIH HHS R01 GM098672NIGMS NIH HHS R21 GM110580NIGMS NIH HHS T32 GM008284
6 · The paper itself

Abstract

Cryo-EM has revealed the structures of many challenging yet exciting macromolecular assemblies at near-atomic resolution (3-4.5Å), providing biological phenomena with molecular descriptions. However, at these resolutions, accurately positioning individual atoms remains challenging and error-prone. Manually refining thousands of amino acids - typical in a macromolecular assembly - is tedious and time-consuming. We present an automated method that can improve the atomic details in models that are manually built in near-atomic-resolution cryo-EM maps. Applying the method to three systems recently solved by cryo-EM, we are able to improve model geometry while maintaining the fit-to-density. Backbone placement errors are automatically detected and corrected, and the refinement shows a large radius of convergence. The results demonstrate that the method is amenable to structures with symmetry, of very large size, and containing RNA as well as covalently bound ligands. The method should streamline the cryo-EM structure determination process, providing accurate and unbiased atomic structure interpretation of such maps.

Indexed as

Automation, LaboratoryComputational BiologyCryoelectron MicroscopyMacromolecular SubstancesMacromolecular Substancesatomic modelsbiophysicscomputational biologycryo-EMmacromolecular assembliesmembrane proteinsnoneRosettastructural biologystructure refinementsystems biology

Identifiers

PMID27669148
PMCPMC5115868

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.