Evidence map›Paper›PMID 18094466›Full record

ArticleActa crystallographica. Section D, Biological crystallography2008

Dealing with structural variability in molecular replacement and crystallographic refinement through normal-mode analysis.

Marc Delarue

Abstract read
In one paragraph

Article in Acta crystallographica. Section D, Biological crystallography, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Review
  5. xMDFF: molecular dynamics flexible fitting of low-resolution X-ray structures.Acta crystallographica. Section D, Biological crystallography · 2014
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Interpretation of very low resolution X-ray electron-density maps using core objects.Acta crystallographica. Section D, Biological crystallography · 2009
    Article
  12. An introduction to molecular replacement.Acta crystallographica. Section D, Biological crystallography · 2008
    Article
  13. BALBES: a molecular-replacement pipeline.Acta crystallographica. Section D, Biological crystallography · 2008
    Article
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

1 author.

Marc DelarueUnité de Dynamique Structurale des Macromolecules, Departement de Biologie Structurale et Chimie, URA 2185 du CNRS, Institut Pasteur, 25 Rue du Dr Roux, 75015 Paris, France. marc.delarue@pasteur.fr

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Normal-mode analysis (NMA) can be used to generate multiple structural variants of a given template model, thereby increasing the chance of finding the molecular-replacement solution. Here, it is shown that it is also possible to directly refine the amplitudes of the normal modes against experimental data (X-ray or cryo-EM), generalizing rigid-body refinement methods by adding just a few additional degrees of freedom that sample collective and large-amplitude movements. It is also argued that the situation where several (conformations of) models are present simultaneously in the crystal can be studied with adjustable occupancies using techniques derived from statistical thermodynamics and already used in molecular modelling.

Indexed as

Computer SimulationAlgorithmsCarrier ProteinsCrystallography, X-RayModels, MolecularProtein ConformationSoftwareCarrier Proteinsglutamine transport proteins

Identifiers

PMID18094466
PMCPMC2394787

What OpenQuestion holds

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Registered trials

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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.