Evidence map›Paper›PMID 28993151›Full record

ArticleBiochimica et biophysica acta. Biomembranes2018

Using a SMALP platform to determine a sub-nm single particle cryo-EM membrane protein structure.

Mayuriben Parmar, Shaun Rawson, Charlotte A Scarff, Adrian Goldman, Timothy R Dafforn, Stephen P Muench, Vincent L G Postis

Open access · hybridAbstract read
In one paragraph

Article in Biochimica et biophysica acta. Biomembranes, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed, 1 pooled it
7.1field-weighted citation impact, top 2% 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

58 citing papers in PubMed, 1 synthesis or guideline pooled it, 111 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. Advances in native cell membrane nanoparticles system.Current opinion in structural biology · 2025
    Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Handling Difficult Cryo-ET Samples: A Study with Primary Neurons from Drosophila melanogaster.Microscopy and microanalysis : the official journal of Microscopy Society of America, Microbeam Analysis Society, Microscopical Society of Canada · 2023
    Article
  15. Review
  16. Characterization of CaBiochimica et biophysica acta. Biomembranes · 2023
    Article
  17. Article
  18. Review
  19. Review
  20. Single-component nanodiscsChemical science · 2022
    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

7 authors at 5 institutions in 2 countries.

Mayuriben ParmarBiomedicine Research Group, Faculty of Health and Social Sciences, Leeds Beckett University, LS1 3HE, UK; School of Biomedical Sciences, Faculty of Biological Sciences, University of Leeds, LS2 9JT, UK.
Shaun RawsonSchool of Biomedical Sciences, Faculty of Biological Sciences, University of Leeds, LS2 9JT, UK; Astbury Centre for Structural Molecular Biology, University of Leeds, LS2 9JT, UK.
Charlotte A ScarffSchool of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, LS2 9JT, UK; Astbury Centre for Structural Molecular Biology, University of Leeds, LS2 9JT, UK.
Adrian GoldmanSchool of Biomedical Sciences, Faculty of Biological Sciences, University of Leeds, LS2 9JT, UK; Astbury Centre for Structural Molecular Biology, University of Leeds, LS2 9JT, UK; Department of Biosciences, Division of Biochemistry, University of Helsinki, Helsinki, Finland.
Timothy R DaffornSchool of Biosciences, University of Birmingham, Edgbaston, Birmingham, B15 2TT, UK.
Stephen P MuenchSchool of Biomedical Sciences, Faculty of Biological Sciences, University of Leeds, LS2 9JT, UK; Astbury Centre for Structural Molecular Biology, University of Leeds, LS2 9JT, UK. Electronic address: s.p.muench@leeds.ac.uk.
Vincent L G PostisBiomedicine Research Group, Faculty of Health and Social Sciences, Leeds Beckett University, LS1 3HE, UK; School of Biomedical Sciences, Faculty of Biological Sciences, University of Leeds, LS2 9JT, UK. Electronic address: V.L.Postis@leedsbeckett.ac.uk.
Institute of Structural and Molecular Biology · GBLeeds Beckett University · GBUniversity of Birmingham · GBUniversity of Helsinki · FIUniversity of Leeds · GB

Funding

Wellcome TrustWellcome Trust 105615/Z/14/Z
6 · The paper itself

Abstract

The field of membrane protein structural biology has been revolutionized over the last few years with a number of high profile structures being solved using cryo-EM including Piezo, Ryanodine receptor, TRPV1 and the Glutamate receptor. Further developments in the EM field hold the promise of even greater progress in terms of greater resolution, which for membrane proteins is still typically within the 4-7Å range. One advantage of a cryo-EM approach is the ability to study membrane proteins in more "native" like environments for example proteoliposomes, amphipols and nanodiscs. Recently, styrene maleic acid co-polymers (SMA) have been used to extract membrane proteins surrounded by native lipids (SMALPs) maintaining a more natural environment. We report here the structure of the Escherichia coli multidrug efflux transporter AcrB in a SMALP scaffold to sub-nm resolution, with the resulting map being consistent with high resolution crystal structures and other EM derived maps. However, both the C-terminal helix (TM12) and TM7 are poorly defined in the map. These helices are at the exterior of the helical bundle and form the greater interaction with the native lipids and SMA polymer and may represent a more dynamic region of the protein. This work shows the promise of using an SMA approach for single particle cryo-EM studies to provide sub-nm structures.

Indexed as

ATP-Binding Cassette, Sub-Family C ProteinsCryoelectron MicroscopyCrystallography, X-RayEscherichia coliEscherichia coli ProteinsLipid BilayersMaleatesMembrane ProteinsModels, MolecularPolystyrenesProtein ConformationProtein MultimerizationProteolipidsAcrB protein, E coliATP-Binding Cassette, Sub-Family C ProteinsEscherichia coli ProteinsLipid BilayersMaleatesMembrane ProteinsPolystyrenesProteolipidsproteoliposomesstyrene-maleic acid polymerAcrBElectron microscopyMembrane proteinsSMALP

Identifiers

PMID28993151
PMCPMC5780298
OpenAlexW2762364099

What OpenQuestion holds

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LicenceCC BY
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.