Evidence map›Paper›PMID 25615869›Full record

ArticleActa crystallographica. Section D, Biological crystallography2015

Structure calculation, refinement and validation using CcpNmr Analysis.

Simon P Skinner, Benjamin T Goult, Rasmus H Fogh, Wayne Boucher, Tim J Stevens, Ernest D Laue, Geerten W Vuister

Abstract readValidation Study
In one paragraph

Article in Acta crystallographica. Section D, Biological crystallography, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing 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

38 citing papers in PubMed.

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  9. The focal adhesion protein talin is a mechanically gated A-kinase anchoring protein.Proceedings of the National Academy of Sciences of the United States of America · 2024
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  14. Evolution avoids a pathological stabilizing interaction in the immune protein S100A9.Proceedings of the National Academy of Sciences of the United States of America · 2022
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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

7 authors.

Simon P SkinnerDepartment of Biochemistry, University of Leicester, Lancaster Road, Leicester LE1 9HN, England.
Benjamin T GoultDepartment of Biochemistry, University of Leicester, Lancaster Road, Leicester LE1 9HN, England.
Rasmus H FoghDepartment of Biochemistry, University of Leicester, Lancaster Road, Leicester LE1 9HN, England.
Wayne BoucherDepartment of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1GA, England.
Tim J StevensCell Biology Division, MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, England.
Ernest D LaueDepartment of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1GA, England.
Geerten W VuisterDepartment of Biochemistry, University of Leicester, Lancaster Road, Leicester LE1 9HN, England.

Funding

Biotechnology and Biological Sciences Research Council BB/E005071/1Biotechnology and Biological Sciences Research Council BB/J007897/1Medical Research Council MC_U105178783Medical Research Council MR/L000555/1
6 · The paper itself

Abstract

CcpNmr Analysis provides a streamlined pipeline for both NMR chemical shift assignment and structure determination of biological macromolecules. In addition, it encompasses tools to analyse the many additional experiments that make NMR such a pivotal technique for research into complex biological questions. This report describes how CcpNmr Analysis can seamlessly link together all of the tasks in the NMR structure-determination process. It details each of the stages from generating NMR restraints [distance, dihedral, hydrogen bonds and residual dipolar couplings (RDCs)], exporting these to and subsequently re-importing them from structure-calculation software (such as the programs CYANA or ARIA) and analysing and validating the results obtained from the structure calculation to, ultimately, the streamlined deposition of the completed assignments and the refined ensemble of structures into the PDBe repository. Until recently, such solution-structure determination by NMR has been quite a laborious task, requiring multiple stages and programs. However, with the new enhancements to CcpNmr Analysis described here, this process is now much more intuitive and efficient and less error-prone.

Indexed as

Hydrogen BondingMolecular StructureNuclear Magnetic Resonance, BiomolecularanalysisCcpNmrNMRprocessingstructure calculationtalin

Identifiers

PMID25615869
PMCPMC4304695

What OpenQuestion holds

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LicenceCC BY
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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.