Evidence map›Paper›PMID 23860256›Full record

ReviewBiochimica et biophysica acta2014

Membrane protein structure determination - the next generation.

Isabel Moraes, Gwyndaf Evans, Juan Sanchez-Weatherby, Simon Newstead, Patrick D Shaw Stewart

Erratum issuedOpen access · hybridAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 107 papers.

0numbers the graph read from it
0cells of the map it votes in
107citing papers in PubMed
9.0field-weighted citation impact, top 1% of its field
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

107 citing papers in PubMed, 241 citations in OpenAlex.

  1. Article
  2. Biomolecular Crystallisation Through Soft Templates and Seeding.Advances in biochemical engineering/biotechnology · 2026
    Review
  3. Review
  4. A tripartite protein complex promotes DNA transport during natural transformation in Firmicutes.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. Article
  6. Article
  7. Challenges of Protein-Protein Docking of the Membrane Proteins.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  8. Pharmaceutical science advances · 2023
    Article
  9. Review
  10. Quantum sensors for biomedical applications.Nature reviews. Physics · 2023
    Review
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Review
  20. Article

47 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 3 institutions in 1 country.

Isabel MoraesDepartment of Life Sciences, Imperial College London, London SW7 2AZ, UK; Membrane Protein Laboratory, Diamond Light Source, Harwell Science and Innovation Campus, Didcot OX11 0DE, UK; Research Complex at Harwell Rutherford Appleton Laboratory, Harwell Science and Innovation Campus, Didcot OX11 0FA, UK. Electronic address: i.moraes@imperial.ac.uk.
Gwyndaf Evans
Juan Sanchez-Weatherby
Simon Newstead
Patrick D Shaw Stewart
Diamond Light Source · GBResearch Complex at Harwell · GBRutherford Appleton Laboratory · GB

Funding

Medical Research Council G0900399Wellcome Trust 099165/Z/12/ZWellcome Trust 102890/Z/13/Z
6 · The paper itself

Abstract

The field of Membrane Protein Structural Biology has grown significantly since its first landmark in 1985 with the first three-dimensional atomic resolution structure of a membrane protein. Nearly twenty-six years later, the crystal structure of the beta2 adrenergic receptor in complex with G protein has contributed to another landmark in the field leading to the 2012 Nobel Prize in Chemistry. At present, more than 350 unique membrane protein structures solved by X-ray crystallography (http://blanco.biomol.uci.edu/mpstruc/exp/list, Stephen White Lab at UC Irvine) are available in the Protein Data Bank. The advent of genomics and proteomics initiatives combined with high-throughput technologies, such as automation, miniaturization, integration and third-generation synchrotrons, has enhanced membrane protein structure determination rate. X-ray crystallography is still the only method capable of providing detailed information on how ligands, cofactors, and ions interact with proteins, and is therefore a powerful tool in biochemistry and drug discovery. Yet the growth of membrane protein crystals suitable for X-ray diffraction studies amazingly remains a fine art and a major bottleneck in the field. It is often necessary to apply as many innovative approaches as possible. In this review we draw attention to the latest methods and strategies for the production of suitable crystals for membrane protein structure determination. In addition we also highlight the impact that third-generation synchrotron radiation has made in the field, summarizing the latest strategies used at synchrotron beamlines for screening and data collection from such demanding crystals. This article is part of a Special Issue entitled: Structural and biophysical characterisation of membrane protein-ligand binding.

Indexed as

Crystallography, X-RayDetergentsMembrane ProteinsProtein ConformationSynchrotronsDetergentsMembrane ProteinsCrystal dehydrationCrystal seedingIn situ data collectionMacromolecular crystallographyMembrane proteinXFEL

Identifiers

PMID23860256
PMCPMC3898769
OpenAlexW2105385262

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

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.