Evidence map›Paper›PMID 20057044›Full record

ArticleActa crystallographica. Section D, Biological crystallography2010

MolProbity: all-atom structure validation for macromolecular crystallography.

Vincent B Chen, W Bryan Arendall, Jeffrey J Headd, Daniel A Keedy, Robert M Immormino, Gary J Kapral, Laura W Murray, Jane S Richardson, David C Richardson

Abstract read
In one paragraph

Article in Acta crystallographica. Section D, Biological crystallography, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9,062 papers.

0numbers the graph read from it
0cells of the map it votes in
9,062citing 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

9,062 citing papers in PubMed.

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  10. Molecular Basis for Activation to Inhibition Switching in Kv7.2 Channel Modulators.Angewandte Chemie (International ed. in English) · 2026
    Article
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  13. Step-by-step maturation mechanism of the binary toxin pore revealed by cryo-EM analysis.Proceedings of the National Academy of Sciences of the United States of America · 2026
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9,002 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

9 authors.

Vincent B ChenDepartment of Biochemistry, Duke University, Durham, NC 27710, USA.
W Bryan Arendall
Jeffrey J Headd
Daniel A Keedy
Robert M Immormino
Gary J Kapral
Laura W Murray
Jane S Richardson
David C Richardson

Funding

MolProbity Validation & Corrections: for Crystallography, PDB & BiomedicineR01GM073919 · NIGMS · DUKE UNIVERSITY · PI RICHARDSON, DAVID CLAUDE · 2006 to 2018
$3.7M
NIGMS NIH HHS GM73919NIGMS NIH HHS R01 GM073919
6 · The paper itself

Abstract

MolProbity is a structure-validation web service that provides broad-spectrum solidly based evaluation of model quality at both the global and local levels for both proteins and nucleic acids. It relies heavily on the power and sensitivity provided by optimized hydrogen placement and all-atom contact analysis, complemented by updated versions of covalent-geometry and torsion-angle criteria. Some of the local corrections can be performed automatically in MolProbity and all of the diagnostics are presented in chart and graphical forms that help guide manual rebuilding. X-ray crystallography provides a wealth of biologically important molecular data in the form of atomic three-dimensional structures of proteins, nucleic acids and increasingly large complexes in multiple forms and states. Advances in automation, in everything from crystallization to data collection to phasing to model building to refinement, have made solving a structure using crystallography easier than ever. However, despite these improvements, local errors that can affect biological interpretation are widespread at low resolution and even high-resolution structures nearly all contain at least a few local errors such as Ramachandran outliers, flipped branched protein side chains and incorrect sugar puckers. It is critical both for the crystallographer and for the end user that there are easy and reliable methods to diagnose and correct these sorts of errors in structures. MolProbity is the authors' contribution to helping solve this problem and this article reviews its general capabilities, reports on recent enhancements and usage, and presents evidence that the resulting improvements are now beneficially affecting the global database.

Indexed as

SoftwareAutomation, LaboratoryCrystallizationCrystallography, X-RayElectronic Data ProcessingNucleic AcidsProteinsQuality ControlReproducibility of ResultsResearch DesignNucleic AcidsProteins

Identifiers

PMID20057044
PMCPMC2803126

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.