Evidence map›Paper›PMID 32709843›Full record

ArticleNature communications2020

Subnanometer-resolution structure determination in situ by hybrid subtomogram averaging - single particle cryo-EM.

Ricardo M Sanchez, Yingyi Zhang, Wenbo Chen, Lea Dietrich, Mikhail Kudryashev

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
5.9field-weighted citation impact, top 4% 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

41 citing papers in PubMed, 68 citations in OpenAlex.

  1. Article
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  5. Article
  6. Structural Analysis of Membrane Proteins in Cell-Derived Microvesicles.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  7. Review
  8. Cryo-EM single-particle analysis expanding towards increasingly native samples.Acta crystallographica. Section D, Structural biology · 2025
    Review
  9. Review
  10. Review
  11. Molecular architecture of synaptic vesicles.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. The big chill: Growth ofQRB discovery · 2024
    Review
  18. Article
  19. Article
  20. 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

5 authors at 2 institutions in 1 country.

Ricardo M Sanchez *Max Planck Institute for Biophysics, Max-von-Laue Strasse, 3, 60348, Frankfurt am Main, Germany.
Yingyi Zhang *Max Planck Institute for Biophysics, Max-von-Laue Strasse, 3, 60348, Frankfurt am Main, Germany.ORCID http://orcid.org/0000-0002-6478-476X
Wenbo ChenMax Planck Institute for Biophysics, Max-von-Laue Strasse, 3, 60348, Frankfurt am Main, Germany.
Lea DietrichDepartment of Structural Biology, Max Planck Institute for Biophysics, Max-von-Laue Strasse, 3, 60348, Frankfurt am Main, Germany.
Mikhail KudryashevMax Planck Institute for Biophysics, Max-von-Laue Strasse, 3, 60348, Frankfurt am Main, Germany. misha.kudryashev@biophys.mpg.de.ORCID http://orcid.org/0000-0003-3550-6274
Goethe University Frankfurt · DEMax Planck Institute of Biophysics · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cryo-electron tomography combined with subtomogram averaging (StA) has yielded high-resolution structures of macromolecules in their native context. However, high-resolution StA is not commonplace due to beam-induced sample drift, images with poor signal-to-noise ratios (SNR), challenges in CTF correction, and limited particle number. Here we address these issues by collecting tilt series with a higher electron dose at the zero-degree tilt. Particles of interest are then located within reconstructed tomograms, processed by conventional StA, and then re-extracted from the high-dose images in 2D. Single particle analysis tools are then applied to refine the 2D particle alignment and generate a reconstruction. Use of our hybrid StA (hStA) workflow improved the resolution for tobacco mosaic virus from 7.2 to 4.4 Å and for the ion channel RyR1 in crowded native membranes from 12.9 to 9.1 Å. These resolution gains make hStA a promising approach for other StA projects aimed at achieving subnanometer resolution.

Indexed as

Calcium ChannelsCryoelectron MicroscopyElectron Microscope TomographyImage Processing, Computer-AssistedMacromolecular SubstancesRyanodine Receptor Calcium Release ChannelSignal-To-Noise RatioSingle Molecule ImagingWorkflowCalcium ChannelsMacromolecular SubstancesRyanodine Receptor Calcium Release Channel

Identifiers

PMID32709843
PMCPMC7381653
OpenAlexW3044117919

What OpenQuestion holds

Textmetadata
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.