Evidence map›Paper›PMID 34099703›Full record

ArticleNature communications2021

Assessment of protein-protein interfaces in cryo-EM derived assemblies.

Sony Malhotra, Agnel Praveen Joseph, Jeyan Thiyagalingam, Maya Topf

Abstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. MultilevelCurrent research in structural biology · 2026
    Article
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  3. Article
  4. Review
  5. Article
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  7. Review of protein structure-based analyses that illuminate plant stress mechanisms.Computational and structural biotechnology journal · 2025
    Review
  8. Article
  9. Article
  10. Article
  11. Glucose-6-phosphate dehydrogenase and its 3D structures from crystallography and electron cryo-microscopy.Acta crystallographica. Section F, Structural biology communications · 2024
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Review
  19. Article
  20. Atomic model validation using the CCP-EM software suite.Acta crystallographica. Section D, Structural biology · 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

4 authors.

Sony MalhotraInstitute of Structural and Molecular Biology, Department of Biological Sciences, Birkbeck College, University of London, London, UK. sony.malhotra@stfc.ac.uk.ORCID http://orcid.org/0000-0002-3165-9081
Agnel Praveen JosephScientific Computing Department, Science and Technology Facilities Council, Didcot, UK.ORCID http://orcid.org/0000-0002-0997-8422
Jeyan ThiyagalingamScientific Computing Department, Science and Technology Facilities Council, Didcot, UK.ORCID http://orcid.org/0000-0002-2167-1343
Maya TopfInstitute of Structural and Molecular Biology, Department of Biological Sciences, Birkbeck College, University of London, London, UK. m.topf@cryst.bbk.ac.uk.ORCID http://orcid.org/0000-0002-8185-1215

Funding

Medical Research Council G0600084Medical Research Council MR/M019292/1Medical Research Council MR/N009614/1Wellcome TrustWellcome Trust 208398/Z/17/ZWellcome Trust 209250/Z/17/Z
6 · The paper itself

Abstract

Structures of macromolecular assemblies derived from cryo-EM maps often contain errors that become more abundant with decreasing resolution. Despite efforts in the cryo-EM community to develop metrics for map and atomistic model validation, thus far, no specific scoring metrics have been applied systematically to assess the interface between the assembly subunits. Here, we comprehensively assessed protein-protein interfaces in macromolecular assemblies derived by cryo-EM. To this end, we developed Protein Interface-score (PI-score), a density-independent machine learning-based metric, trained using the features of protein-protein interfaces in crystal structures. We evaluated 5873 interfaces in 1053 PDB-deposited cryo-EM models (including SARS-CoV-2 complexes), as well as the models submitted to CASP13 cryo-EM targets and the EM model challenge. We further inspected the interfaces associated with low-scores and found that some of those, especially in intermediate-to-low resolution (worse than 4 Å) structures, were not captured by density-based assessment scores. A combined score incorporating PI-score and fit-to-density score showed discriminatory power, allowing our method to provide a powerful complementary assessment tool for the ever-increasing number of complexes solved by cryo-EM.

Indexed as

Protein Interaction Domains and MotifsProtein Interaction MapsCryoelectron MicroscopyHumansMachine LearningMacromolecular SubstancesModels, MolecularNeural Networks, ComputerProtein ConformationProtein Interaction MappingProtein MultimerizationProteinsSupport Vector MachineViral Nonstructural ProteinsMacromolecular SubstancesORF1ab polyprotein, SARS-CoV-2ProteinsViral Nonstructural Proteins

Identifiers

PMID34099703
PMCPMC8184972

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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.