Evidence map›Paper›PMID 20693688›Full record

ArticleActa crystallographica. Section D, Biological crystallography2010

Validation of crystallographic models containing TLS or other descriptions of anisotropy.

Frank Zucker, P Christoph Champ, Ethan A Merritt

Abstract readValidation Study
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 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing 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

44 citing papers in PubMed.

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  10. Optimal structure determination from sub-optimal diffraction data.Protein science : a publication of the Protein Society · 2022
    Article
  11. B-factor accuracy in protein crystal structures.Acta crystallographica. Section D, Structural biology · 2022
    Article
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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

3 authors.

Frank ZuckerBiomolecular Structure Center, Department of Biochemistry, University of Washington, Seattle, WA 98195-7742, USA.
P Christoph Champ
Ethan A Merritt

Funding

Software tools for analysis and visulaization of protein structureR01GM080232 · NIGMS · UNIVERSITY OF WASHINGTON · PI MERRITT, ETHAN A · 2007 to 2010
$1.1M
NCI NIH HHS Y1-CO-1020NIGMS NIH HHS R01 GM080232NIGMS NIH HHS R01GM080232NIGMS NIH HHS Y1-GM-1104
6 · The paper itself

Abstract

The use of TLS (translation/libration/screw) models to describe anisotropic displacement of atoms within a protein crystal structure has become increasingly common. These models may be used purely as an improved methodology for crystallographic refinement or as the basis for analyzing inter-domain and other large-scale motions implied by the crystal structure. In either case it is desirable to validate that the crystallographic model, including the TLS description of anisotropy, conforms to our best understanding of protein structures and their modes of flexibility. A set of validation tests has been implemented that can be integrated into ongoing crystallographic refinement or run afterwards to evaluate a previously refined structure. In either case validation can serve to increase confidence that the model is correct, to highlight aspects of the model that may be improved or to strengthen the evidence supporting specific modes of flexibility inferred from the refined TLS model. Automated validation checks have been added to the PARVATI and TLSMD web servers and incorporated into the CCP4i user interface.

Indexed as

AnisotropyCrystallography, X-RayDatabases, ProteinInternetModels, Chemical

Identifiers

PMID20693688
PMCPMC2917275

What OpenQuestion holds

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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.