Evidence map›Paper›PMID 34990602›Full record

ArticleStructure (London, England : 1993)2022

Quantitative mining of compositional heterogeneity in cryo-EM datasets of ribosome assembly intermediates.

Jessica N Rabuck-Gibbons, Dmitry Lyumkis, James R Williamson

Abstract read
In one paragraph

Article in Structure (London, England : 1993), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed.

  1. Article
  2. Article
  3. How many (distinguishable) classes can we identify in single-particle analysis?Acta crystallographica. Section D, Structural biology · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. Autonomous ribosome biogenesis in vitro.Nature communications · 2025
    Article
  8. Article
  9. Article
  10. Automated model-free analysis of cryo-EM volume ensembles with SIREn.bioRxiv : the preprint server for biology · 2024
    Article
  11. Article
  12. Article
  13. Review
  14. Assembly of the Bacterial Ribosome with Circularly Permuted rRNA.bioRxiv : the preprint server for biology · 2024
    Article
  15. Article
  16. Structural Analysis of Protein Complexes by Cryo-Electron Microscopy.Methods in molecular biology (Clifton, N.J.) · 2024
    Review
  17. Article
  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

3 authors.

Jessica N Rabuck-GibbonsDepartment of Integrative Structural and Computational Biology, Department of Chemistry, and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
Dmitry LyumkisDepartment of Integrative Structural and Computational Biology, Department of Chemistry, and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA; Laboratory of Genetics and Helmsley Center for Genomic Medicine, The Salk Institute for Biological Studies, La Jolla, CA 92037, USA.
James R WilliamsonDepartment of Integrative Structural and Computational Biology, Department of Chemistry, and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA. Electronic address: jrwill@scripps.edu.

Funding

X-ray Crystallographic Fragment Screening CoreU54AI150472 · NIAID · SEATTLE CHILDREN'S HOSPITAL · PI LYUMKIS, DMITRY · 2019 to 2021
$15.7M
Resource for Biocomputing Visualization and InformaticsP41GM103311 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FERRIN, THOMAS E · 2012 to 2017
$8.2M
STRUCTURE AND ASSEMBLY OF 30 S CENTRAL DOMAIN RNPSR01GM053757 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI WILLIAMSON, JAMES R · 1996 to 2020
$5.0M
Dynamics of the Bacterial Ribosome and Proteome (Equipment Supplement)R35GM136412 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI James R Williamson · 2020 to 2026
$4.9M
Breaking Barriers in Structural Biology: Novel CryoEM Methods and ApplicationsDP5OD021396 · OD · SALK INSTITUTE FOR BIOLOGICAL STUDIES · PI LYUMKIS, DMITRY · 2015 to 2019
$2.4M
NIAID NIH HHS U54 AI150472NIGMS NIH HHS P41 GM103311NIGMS NIH HHS R01 GM053757NIGMS NIH HHS R35 GM136412NIH HHS DP5 OD021396
6 · The paper itself

Abstract

Single-particle cryoelectron microscopy (cryo-EM) offers a unique opportunity to characterize macromolecular structural heterogeneity by virtue of its ability to place distinct particle populations into different groups through computational classification. However, there is a dearth of tools for surveying the heterogeneity landscape, quantitatively analyzing heterogeneous particle populations after classification, deciding how many unique classes are represented by the data, and accurately cross-comparing reconstructions. Here, we develop a workflow that contains discovery and analysis modules to quantitatively mine cryo-EM data for sets of structures with maximal diversity. This workflow was applied to a dataset of E. coli 50S ribosome assembly intermediates, which are characterized by significant structural heterogeneity. We identified more detailed branchpoints in the assembly process and characterized the interactions of an assembly factor with immature intermediates. While the tools described here were developed for ribosome assembly, they should be broadly applicable to the analysis of other heterogeneous cryo-EM datasets.

Indexed as

Escherichia coliRibosomesCryoelectron MicroscopyMacromolecular SubstancesMacromolecular Substancesclassificationcryoelectron microscopyheterogeneity analysisribosome biogenesissingle-particle analysis

Identifiers

PMID34990602
PMCPMC9891661

What OpenQuestion holds

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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.