Evidence map›Paper›PMID 24507780›Full record

ArticleStructure (London, England : 1993)2014

Diffuse X-ray scattering to model protein motions.

Michael E Wall, Paul D Adams, James S Fraser, Nicholas K Sauter

Abstract readConference Proceedings
In one paragraph

Article in Structure (London, England : 1993), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Bringing diffuse X-ray scattering into focus.Current opinion in structural biology · 2018
    Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Measuring and modeling diffuse scattering in protein X-ray crystallography.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  12. Article
  13. Article
  14. Acoustic vibrations contribute to the diffuse scatter produced by ribosome crystals.Acta crystallographica. Section D, Biological crystallography · 2015
    Article
  15. Predicting X-ray diffuse scattering from translation-libration-screw structural ensembles.Acta crystallographica. Section D, Biological crystallography · 2015
    Article
  16. The solvent component of macromolecular crystals.Acta crystallographica. Section D, Biological crystallography · 2015
    Review
  17. Review
  18. Review
  19. Article
  20. E pluribus unum, no more: from one crystal, many conformations.Current opinion in structural biology · 2014
    Review
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

4 authors.

Michael E WallComputer, Computational, and Statistical Sciences Division, Los Alamos National Laboratory, Los Alamos, NM 87545, USA. Electronic address: mewall@lanl.gov.
Paul D AdamsPhysical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA; Department of Bioengineering, University of California, Berkeley, Berkeley, CA 94720, USA.
James S FraserDepartment of Bioengineering and Therapeutic Sciences, University of California, San Francisco, San Francisco, CA 94143, USA.
Nicholas K SauterPhysical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.

Funding

PROJECT 5 - DUKE - STRUCTURE VALIDATION AND IMPROVEMENT FOR PROTEINS AND N. ACIDSP01GM063210 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI ADAMS, PAUL DAVID · 2001 to 2021
$33.5M
The Impact of Mutation on the Conformations and Recognition of UbiquitinDP5OD009180 · OD · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FRASER, JAMES SOLOMON · 2011 to 2015
$1.8M
Realizing New Horizons in X-ray Crystallography Data ProcessingR01GM095887 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI SAUTER, NICHOLAS K · 2011 to 2014
$1.5M
NIGMS NIH HHS 1P01GM063210NIGMS NIH HHS GM095887NIGMS NIH HHS P01 GM063210NIGMS NIH HHS R01 GM095887NIH HHS DP5 OD009180NIH HHS DP5OD009180
6 · The paper itself

Abstract

Problems in biology increasingly need models of protein flexibility to understand and control protein function. At the same time, as they improve, crystallographic methods are marching closer to the limits of what can be learned from Bragg data in isolation. It is thus inevitable that mainstream protein crystallography will turn to diffuse scattering to model protein motions and improve crystallographic models. The time is ripe to make it happen.

Indexed as

CaliforniaCrystallography, X-RayMolecular Dynamics SimulationMotionProtein ConformationProteinsScattering, RadiationX-RaysProteins

Identifiers

PMID24507780
PMCPMC4070675

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.