Evidence map›Paper›PMID 21296162›Full record

ArticleJournal of structural biology2011

Modeling protein structure at near atomic resolutions with Gorgon.

Matthew L Baker, Sasakthi S Abeysinghe, Stephen Schuh, Ross A Coleman, Austin Abrams, Michael P Marsh, Corey F Hryc, Troy Ruths, Wah Chiu, Tao Ju

Abstract read
In one paragraph

Article in Journal of structural biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing 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

54 citing papers in PubMed.

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  15. Combine Cryo-EM Density Map and Residue Contact for Protein Structure Prediction - A Case Study.ACM-BCB ... ... : the ... ACM Conference on Bioinformatics, Computational Biology and Biomedicine. ACM Conference on Bioinformatics, Computational Biology and Biomedicine · 2020
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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

10 authors.

Matthew L BakerNational Center for Macromolecular Imaging, Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, USA. mbaker@bcm.edu
Sasakthi S Abeysinghe
Stephen Schuh
Ross A Coleman
Austin Abrams
Michael P Marsh
Corey F Hryc
Troy Ruths
Wah Chiu
Tao Ju

Funding

ZERNIKE PHASE PLATE CRYOEM IN OKAZAKIP41RR002250 · NCRR · UNIVERSITY OF ARIZONA · PI CHIU, WAH · 1985 to 2011
$22.1M
Unified Data Resource for Large Complexes Determined by Cryo-Electron MicroscopyR01GM079429 · NIGMS · STANFORD UNIVERSITY · PI CHIU, WAH · 2007 to 2021
$11.6M
Training in Biomedical Discovery from Large Scale Data SetsT90DA022885 · NIDA · BAYLOR COLLEGE OF MEDICINE · PI PALZKILL, TIMOTHY · 2006 to 2009
$635k
NCRR NIH HHS P41 RR002250NCRR NIH HHS P41RR002250NIDA NIH HHS 1 T90DA022885-01NIDA NIH HHS T90 DA022885NIGMS NIH HHS R01 GM079429NIGMS NIH HHS R01GM079429
6 · The paper itself

Abstract

Electron cryo-microscopy (cryo-EM) has played an increasingly important role in elucidating the structure and function of macromolecular assemblies in near native solution conditions. Typically, however, only non-atomic resolution reconstructions have been obtained for these large complexes, necessitating computational tools for integrating and extracting structural details. With recent advances in cryo-EM, maps at near-atomic resolutions have been achieved for several macromolecular assemblies from which models have been manually constructed. In this work, we describe a new interactive modeling toolkit called Gorgon targeted at intermediate to near-atomic resolution density maps (10-3.5 Å), particularly from cryo-EM. Gorgon's de novo modeling procedure couples sequence-based secondary structure prediction with feature detection and geometric modeling techniques to generate initial protein backbone models. Beyond model building, Gorgon is an extensible interactive visualization platform with a variety of computational tools for annotating a wide variety of 3D volumes. Examples from cryo-EM maps of Rotavirus and Rice Dwarf Virus are used to demonstrate its applicability to modeling protein structure.

Indexed as

Models, MolecularProtein ConformationSoftwareAmino Acid SequenceAntigens, ViralCapsid ProteinsComputer SimulationCryoelectron MicroscopyData DisplayMolecular Sequence DataProteinsAntigens, ViralCapsid ProteinsProteinsVP6 protein, Rotavirus

Identifiers

PMID21296162
PMCPMC3078171

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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.