Evidence map›Paper›PMID 26057664›Full record

ArticleActa crystallographica. Section D, Biological crystallography2015

Structure determination of an integral membrane protein at room temperature from crystals in situ.

Danny Axford, James Foadi, Nien Jen Hu, Hassanul Ghani Choudhury, So Iwata, Konstantinos Beis, Gwyndaf Evans, Yilmaz Alguel

Abstract read
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 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing 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

26 citing papers in PubMed.

  1. High-Resolution Cryo-Electron Microscopy Structure Determination ofInternational journal of molecular sciences · 2024
    Article
  2. Article
  3. xia2.multiplex: a multi-crystal data-analysis pipeline.Acta crystallographica. Section D, Structural biology · 2022
    Article
  4. Article
  5. Review
  6. Low-doseIUCrJ · 2020
    Article
  7. High-throughput in situ experimental phasing.Acta crystallographica. Section D, Structural biology · 2020
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Review
  16. Signatures of Mechanosensitive Gating.Biophysical journal · 2017
    Article
  17. Article
  18. Article
  19. Review
  20. Applications of thin-film sandwich crystallization platforms.Acta crystallographica. Section F, Structural biology communications · 2016
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors.

Danny AxfordDiamond Light Source, Harwell Science and Innovation Campus, Oxfordshire OX11 0DE, England.
James FoadiMembrane Protein Laboratory, Diamond Light Source, Harwell Science and Innovation Campus, Oxfordshire OX11 0DE, England.
Nien Jen HuMembrane Protein Laboratory, Diamond Light Source, Harwell Science and Innovation Campus, Oxfordshire OX11 0DE, England.
Hassanul Ghani ChoudhuryMembrane Protein Laboratory, Diamond Light Source, Harwell Science and Innovation Campus, Oxfordshire OX11 0DE, England.
So IwataDiamond Light Source, Harwell Science and Innovation Campus, Oxfordshire OX11 0DE, England.
Konstantinos BeisMembrane Protein Laboratory, Diamond Light Source, Harwell Science and Innovation Campus, Oxfordshire OX11 0DE, England.
Gwyndaf EvansDiamond Light Source, Harwell Science and Innovation Campus, Oxfordshire OX11 0DE, England.
Yilmaz AlguelMembrane Protein Laboratory, Diamond Light Source, Harwell Science and Innovation Campus, Oxfordshire OX11 0DE, England.

Funding

Biotechnology and Biological Sciences Research Council BB/G023425/1Wellcome TrustWellcome Trust WT/099165/Z/12/Z
6 · The paper itself

Abstract

The structure determination of an integral membrane protein using synchrotron X-ray diffraction data collected at room temperature directly in vapour-diffusion crystallization plates (in situ) is demonstrated. Exposing the crystals in situ eliminates manual sample handling and, since it is performed at room temperature, removes the complication of cryoprotection and potential structural anomalies induced by sample cryocooling. Essential to the method is the ability to limit radiation damage by recording a small amount of data per sample from many samples and subsequently assembling the resulting data sets using specialized software. The validity of this procedure is established by the structure determination of Haemophilus influenza TehA at 2.3 Å resolution. The method presented offers an effective protocol for the fast and efficient determination of membrane-protein structures at room temperature using third-generation synchrotron beamlines.

Indexed as

Bacterial ProteinsCrystallography, X-RayHaemophilus influenzaeMembrane ProteinsModels, MolecularProtein ConformationTemperatureBacterial ProteinsMembrane Proteinsin situ data collectionmembrane proteinmultiple data setssynchrotron beamline

Identifiers

PMID26057664
PMCPMC4461203

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.