Evidence map›Paper›PMID 35913392›Full record

ArticleFaraday discussions2022

Cryomicroscopy

Christopher J Russo, Joshua L Dickerson, Katerina Naydenova

Open access · hybridAbstract read
In one paragraph

Article in Faraday discussions, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
8.5field-weighted citation impact, top 3% 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

17 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Characterization Standard forbioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Article
  5. Cryo-EM single-particle analysis expanding towards increasingly native samples.Acta crystallographica. Section D, Structural biology · 2025
    Review
  6. Ultracold cryogenic TEM with liquid helium and high stability.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Article
  8. Cryo-EM structures of apo and atorvastatin-bound human 3-hydroxy-3-methylglutaryl-coenzyme A reductase.Acta crystallographica. Section F, Structural biology communications · 2025
    Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Automated model building and protein identification in cryo-EM maps.bioRxiv : the preprint server for biology · 2023
    Article
  17. Quantification of gallium cryo-FIB milling damage in biological lamellae.Proceedings of the National Academy of Sciences of the United States of America · 2023
    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

3 authors at 1 institution in 1 country.

Christopher J RussoMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 0QH, UK. crusso@mrc-lmb.cam.ac.uk.ORCID 0000-0002-4442-744X
Joshua L DickersonMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 0QH, UK. crusso@mrc-lmb.cam.ac.uk.ORCID 0000-0001-5049-4000
Katerina NaydenovaMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 0QH, UK. crusso@mrc-lmb.cam.ac.uk.ORCID 0000-0001-5533-5930
MRC Laboratory of Molecular Biology · GB

Funding

Medical Research Council MC_UP_1201/17Medical Research Council MC_UP_120117Wellcome TrustWellcome Trust 220526/B/20/Z
6 · The paper itself

Abstract

Electron cryomicroscopy (cryoEM) has made great strides in the last decade, such that the atomic structure of most biological macromolecules can, at least in principle, be determined. Major technological advances - in electron imaging hardware, data analysis software, and cryogenic specimen preparation technology - continue at pace and contribute to the exponential growth in the number of atomic structures determined by cryoEM. It is now conceivable that within the next decade we will have structures for hundreds of thousands of unique protein and nucleic acid molecular complexes. But the answers to many important questions in biology would become obvious if we could identify these structures precisely inside cells with quantifiable error. In the context of an abundance of known structures, it is appropriate to consider the current state of electron cryomicroscopy for frozen specimens prepared directly from cells, and try to answer to the question of the title, both now and in the foreseeable future.

Indexed as

ProteinsSoftwareCryoelectron MicroscopyProteins

Identifiers

PMID35913392
PMCPMC9642008
OpenAlexW4289356783

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.