Evidence map›Paper›PMID 33397925›Full record

ArticleNature communications2021

FSC-Q: a CryoEM map-to-atomic model quality validation based on the local Fourier shell correlation.

Erney Ramírez-Aportela, David Maluenda, Yunior C Fonseca, Pablo Conesa, Roberto Marabini, J Bernard Heymann, Jose Maria Carazo, Carlos Oscar S Sorzano

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 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing 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

27 citing papers in PubMed.

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  5. Structural mechanism for the recognition of E2F1 by the ubiquitin ligase adaptor Cyclin F.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Review
  7. Review
  8. Review
  9. A Visual Environment for Data Driven Protein Modeling and Validation.IEEE transactions on visualization and computer graphics · 2024
    Article
  10. Article
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  15. Using deep-learning predictions of inter-residue distances for model validation.Acta crystallographica. Section D, Structural biology · 2022
    Article
  16. Review
  17. Article
  18. Article
  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

8 authors.

Erney Ramírez-AportelaBiocomputing Unit, National Center for Biotechnology (CSIC), Darwin 3, Campus Univ. Autónoma de Madrid, Cantoblanco, 28049, Madrid, Spain. erney.ramirez@gmail.com.ORCID 0000-0002-8124-5004
David MaluendaBiocomputing Unit, National Center for Biotechnology (CSIC), Darwin 3, Campus Univ. Autónoma de Madrid, Cantoblanco, 28049, Madrid, Spain.
Yunior C FonsecaBiocomputing Unit, National Center for Biotechnology (CSIC), Darwin 3, Campus Univ. Autónoma de Madrid, Cantoblanco, 28049, Madrid, Spain.
Pablo ConesaBiocomputing Unit, National Center for Biotechnology (CSIC), Darwin 3, Campus Univ. Autónoma de Madrid, Cantoblanco, 28049, Madrid, Spain.
Roberto MarabiniUniv. Autónoma de Madrid, Campus Univ. Autónoma de Madrid, Cantoblanco, 28049, Madrid, Spain.
J Bernard HeymannLaboratory of Structural Biology Research, NIAMS, NIH, Bethesda, MD, USA.ORCID 0000-0002-8872-5326
Jose Maria CarazoBiocomputing Unit, National Center for Biotechnology (CSIC), Darwin 3, Campus Univ. Autónoma de Madrid, Cantoblanco, 28049, Madrid, Spain. carazo@cnb.csic.es.ORCID 0000-0003-0788-8447
Carlos Oscar S SorzanoBiocomputing Unit, National Center for Biotechnology (CSIC), Darwin 3, Campus Univ. Autónoma de Madrid, Cantoblanco, 28049, Madrid, Spain. coss@cnb.csic.es.ORCID 0000-0002-9473-283X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In recent years, advances in cryoEM have dramatically increased the resolution of reconstructions and, with it, the number of solved atomic models. It is widely accepted that the quality of cryoEM maps varies locally; therefore, the evaluation of the maps-derived structural models must be done locally as well. In this article, a method for the local analysis of the map-to-model fit is presented. The algorithm uses a comparison of two local resolution maps. The first is the local FSC (Fourier shell correlation) between the full map and the model, while the second is calculated between the half maps normally used in typical single particle analysis workflows. We call the quality measure "FSC-Q", and it is a quantitative estimation of how much of the model is supported by the signal content of the map. Furthermore, we show that FSC-Q may be helpful to detect overfitting. It can be used to complement other methods, such as the Q-score method that estimates the resolvability of atoms.

Indexed as

AlgorithmsCryoelectron MicroscopyFourier AnalysisModels, MolecularReceptors, G-Protein-CoupledSpike Glycoprotein, CoronavirusReceptors, G-Protein-CoupledSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2

Identifiers

PMID33397925
PMCPMC7782520

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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.