Evidence map›Paper›PMID 36841832›Full record

ArticleNature communications2023

The translating bacterial ribosome at 1.55 Å resolution generated by cryo-EM imaging services.

Simon A Fromm, Kate M O'Connor, Michael Purdy, Pramod R Bhatt, Gary Loughran, John F Atkins, Ahmad Jomaa, Simone Mattei

Abstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing 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

44 citing papers in PubMed.

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  9. Transient ion-mediated interactions regulate subunit rotation in a eukaryotic ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  19. Extending the reach of single-particle cryoEM.Current opinion in structural biology · 2025
    Review
  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

8 authors.

Simon A Fromm *EMBL Imaging Centre, European Molecular Biology Laboratory, Meyerhofstraße 1, 69117, Heidelberg, Germany.ORCID 0000-0002-2094-1911
Kate M O'ConnorSchool of Biochemistry and Cell Biology, University College Cork, Cork, T12 XF62, Ireland.ORCID 0000-0002-4862-4918
Michael PurdyDepartment of Molecular Physiology and Biological Physics, School of Medicine, University of Virginia, Charlottesville, VA, USA.
Pramod R BhattSchool of Biochemistry and Cell Biology, University College Cork, Cork, T12 XF62, Ireland.
Gary LoughranSchool of Biochemistry and Cell Biology, University College Cork, Cork, T12 XF62, Ireland.
John F AtkinsSchool of Biochemistry and Cell Biology, University College Cork, Cork, T12 XF62, Ireland. J.Atkins@ucc.ie.ORCID 0000-0001-7933-0165
Ahmad Jomaa *Department of Molecular Physiology and Biological Physics, School of Medicine, University of Virginia, Charlottesville, VA, USA. ahmadjomaa@virginia.edu.ORCID 0000-0002-5543-7942
Simone MatteiEMBL Imaging Centre, European Molecular Biology Laboratory, Meyerhofstraße 1, 69117, Heidelberg, Germany. simone.mattei@embl.de.ORCID 0000-0002-2005-8977

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Our understanding of protein synthesis has been conceptualised around the structure and function of the bacterial ribosome. This complex macromolecular machine is the target of important antimicrobial drugs, an integral line of defence against infectious diseases. Here, we describe how open access to cryo-electron microscopy facilities combined with bespoke user support enabled structural determination of the translating ribosome from Escherichia coli at 1.55 Å resolution. The obtained structures allow for direct determination of the rRNA sequence to identify ribosome polymorphism sites in the E. coli strain used in this study and enable interpretation of the ribosomal active and peripheral sites at unprecedented resolution. This includes scarcely populated chimeric hybrid states of the ribosome engaged in several tRNA translocation steps resolved at ~2 Å resolution. The current map not only improves our understanding of protein synthesis but also allows for more precise structure-based drug design of antibiotics to tackle rising bacterial resistance.

Indexed as

Escherichia coliRibosomesBacteriaCryoelectron MicroscopyModels, MolecularRNA, RibosomalRNA, Ribosomal

Identifiers

PMID36841832
PMCPMC9968351

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Registered trials

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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.