Evidence map›Paper›PMID 22696403›Full record

ArticleBiopolymers2012

Gorgon and pathwalking: macromolecular modeling tools for subnanometer resolution density maps.

Matthew L Baker, Mariah R Baker, Corey F Hryc, Tao Ju, Wah Chiu

Open access · bronzeAbstract read
In one paragraph

Article in Biopolymers, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
5.1field-weighted citation impact, top 5% of its field
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

23 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
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  4. Validation, analysis and annotation of cryo-EM structures.Acta crystallographica. Section D, Structural biology · 2021
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  19. Numerical geometry of map and model assessment.Journal of structural biology · 2015
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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

5 authors at 2 institutions in 1 country.

Matthew L BakerVerna and Marrs McLean Department of Biochemistry and Molecular Biology, National Center for Macromolecular Imaging, Baylor College of Medicine, Houston, TX 77030, USA. mbaker@bcm.edu
Mariah R Baker
Corey F Hryc
Tao Ju
Wah Chiu
Baylor College of Medicine · USWashington University in St. Louis · US

Funding

ZERNIKE PHASE PLATE CRYOEM IN OKAZAKIP41RR002250 · NCRR · UNIVERSITY OF ARIZONA · PI JOACHIMIAK, ANDRZEJ · 1985 to 2011
$22.1M
TRAINING PROGRAM IN COMPUTATIONAL BIOLOGY AND MEDICINET15LM007093 · NLM · RICE UNIVERSITY · PI Lydia E. Kavraki · 1992 to 2026
$20.8M
Unified Data Resource for Large Complexes Determined by Cryo-Electron MicroscopyR01GM079429 · NIGMS · STANFORD UNIVERSITY · PI CHIU, WAH · 2007 to 2021
$11.6M
NCRR NIH HHS P41 RR002250NCRR NIH HHS P41RR002250NIGMS NIH HHS R01 GM079429NIGMS NIH HHS R01GM079429NLM NIH HHS T15 LM007093NLM NIH HHS T15LM007093
6 · The paper itself

Abstract

The complex interplay of proteins and other molecules, often in the form of large transitory assemblies, are critical to cellular function. Today, X-ray crystallography and electron cryo-microscopy (cryo-EM) are routinely used to image these macromolecular complexes, though often at limited resolutions. Despite the rapidly growing number of macromolecular structures, few tools exist for modeling and annotating structures in the range of 3-10 Å resolution. To address this need, we have developed a number of utilities specifically targeting subnanometer resolution density maps. As part of the 2010 Cryo-EM Modeling Challenge, we demonstrated two of our latest de novo modeling tools, Pathwalking and Gorgon, as well as a tool for secondary structure identification (SSEHunter) and a new rigid-body/flexible fitting tool in Gorgon. In total, we submitted 30 structural models from ten different subnanometer resolution data sets in four of the six challenge categories. Each of our utlities produced accurate structural models and annotations across the various density maps. In the end, the utilities that we present here offer users a robust toolkit for analyzing and modeling protein structure in macromolecular assemblies at non-atomic resolutions.

Indexed as

Models, MolecularCryoelectron MicroscopyNanotechnologyProteinsProtein Structure, SecondaryProteins

Identifiers

PMID22696403
PMCPMC3899894
OpenAlexW2009061886

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

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.