Evidence map›Paper›PMID 21893283›Full record

ArticleStructure (London, England : 1993)2011

Symmetry-restrained flexible fitting for symmetric EM maps.

Kwok-Yan Chan, James Gumbart, Ryan McGreevy, Jean M Watermeyer, B Trevor Sewell, Klaus Schulten

Abstract read
In one paragraph

Article in Structure (London, England : 1993), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing 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

51 citing papers in PubMed.

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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.

Kwok-Yan ChanDepartment of Physics, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.
James Gumbart
Ryan McGreevy
Jean M Watermeyer
B Trevor Sewell
Klaus Schulten

Funding

WHOLE CELL SIMULATIONP41RR005969 · NCRR · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI STONE, JOHN H · 1990 to 2011
$19.8M
NCRR NIH HHS P41 RR005969NCRR NIH HHS P41-RR005969
6 · The paper itself

Abstract

Many large biological macromolecules have inherent structural symmetry, being composed of a few distinct subunits, repeated in a symmetric array. These complexes are often not amenable to traditional high-resolution structural determination methods, but can be imaged in functionally relevant states using cryo-electron microscopy (cryo-EM). A number of methods for fitting atomic-scale structures into cryo-EM maps have been developed, including the molecular dynamics flexible fitting (MDFF) method. However, quality and resolution of the cryo-EM map are the major determinants of a method's success. In order to incorporate knowledge of structural symmetry into the fitting procedure, we developed the symmetry-restrained MDFF method. The new method adds to the cryo-EM map-derived potential further restraints on the allowed conformations of a complex during fitting, thereby improving the quality of the resultant structure. The benefit of using symmetry-based restraints during fitting, particularly for medium to low-resolution data, is demonstrated for three different systems.

Indexed as

Data Interpretation, StatisticalMolecular Dynamics SimulationAlgorithmsAminohydrolasesBacterial ProteinsChaperonin 10Chaperonin 60Cryoelectron MicroscopyGroup II ChaperoninsProtein ConformationAminohydrolasesBacterial ProteinsChaperonin 10Chaperonin 60Group II Chaperoninsnitrilase

Identifiers

PMID21893283
PMCPMC3412758

What OpenQuestion holds

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Registered trials

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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.