Evidence map›Paper›PMID 30449687›Full record

ArticleStructure (London, England : 1993)2019

A Multi-model Approach to Assessing Local and Global Cryo-EM Map Quality.

Mark A Herzik, James S Fraser, Gabriel C Lander

Abstract read
In one paragraph

Article in Structure (London, England : 1993), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing 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

43 citing papers in PubMed.

  1. Article
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  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Validation, analysis and annotation of cryo-EM structures.Acta crystallographica. Section D, Structural biology · 2021
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. The accuracy of protein models automatically built into cryo-EM maps with ARP/wARP.Acta crystallographica. Section D, Structural biology · 2021
    Article
  19. Review
  20. Automated Modeling and Validation of Protein Complexes in Cryo-EM Maps.Methods in molecular biology (Clifton, N.J.) · 2021
    Review
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.

Mark A HerzikDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
James S FraserDepartment of Bioengineering and Therapeutic Science and California Institute for Quantitative Biology, University of California, San Francisco, San Francisco, CA, USA.
Gabriel C LanderDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA. Electronic address: glander@scripps.edu.

Funding

PROJECT 5 - DUKE - STRUCTURE VALIDATION AND IMPROVEMENT FOR PROTEINS AND N. ACIDSP01GM063210 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI ADAMS, PAUL DAVID · 2001 to 2021
$33.5M
Molecular basis of axonal transport described by high-resolution 3D imagingDP2EB020402 · NIBIB · SCRIPPS RESEARCH INSTITUTE, THE · PI LANDER, GABRIEL C · 2014 to 2014
$2.8M
Supplement to Resolving ensemble averaged conformations by multi-temperature x-ray crystallography - Equipment 2020R01GM123159 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FRASER, JAMES SOLOMON · 2018 to 2021
$2.3M
COMPUTING AND DATA STORAGE CLUSTER FOR ELECTRON MICROSCOPYS10OD021634 · OD · SCRIPPS RESEARCH INSTITUTE, THE · PI LANDER, GABRIEL C · 2016 to 2016
$531k
NIBIB NIH HHS DP2 EB020402NIGMS NIH HHS P01 GM063210NIH HHS S10 OD021634
6 · The paper itself

Abstract

There does not currently exist a standardized indicator of how well cryo-EM-derived models represent the density from which they were generated. We present a straightforward methodology that utilizes freely available tools to generate a suite of independent models and to evaluate their convergence in an EM density. These analyses provide both a quantitative and qualitative assessment of the precision of the models and their representation of the density, respectively, while concurrently providing a platform for assessing both global and local EM map quality. We further use standardized datasets to provide an expected deviation within a suite of models refined against EM maps reported to be at 5 Å resolution or better. Associating multiple atomic models with a deposited EM map provides a rapid and accessible reporter of convergence, a strong indicator of highly resolved molecular detail, and is an important step toward an FSC-independent assessment of map and model quality.

Indexed as

Cryoelectron MicroscopyModels, MolecularProtein ConformationProteinsSoftwareProteinsatomic modelingcryo-EMvalidation

Identifiers

PMID30449687
PMCPMC6365196

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.