Evidence map›Paper›PMID 31599033›Full record

ArticleProtein science : a publication of the Protein Society2020

Cryo-EM map interpretation and protein model-building using iterative map segmentation.

Thomas C Terwilliger, Paul D Adams, Pavel V Afonine, Oleg V Sobolev

Open access · hybridAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2020. 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
4.2field-weighted citation impact, top 6% of its field
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, 37 citations in OpenAlex.

  1. Article
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  7. Recognizing amino acid sidechains in a medium-resolution cryo-electron density map.Protein science : a publication of the Protein Society · 2025
    Article
  8. Review
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  14. Review
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  16. Redeployment of automated MrBUMP search-model identification for map fitting in cryo-EM.Acta crystallographica. Section D, Structural biology · 2021
    Article
  17. Article
  18. CERES: a cryo-EM re-refinement system for continuous improvement of deposited models.Acta crystallographica. Section D, Structural biology · 2021
    Article
  19. Article
  20. 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

4 authors at 2 institutions in 1 country.

Thomas C TerwilligerLos Alamos National Laboratory, Los Alamos, New Mexico.ORCID 0000-0001-6384-0320
Paul D AdamsMolecular Biophysics & Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, California.
Pavel V AfonineMolecular Biophysics & Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, California.
Oleg V SobolevMolecular Biophysics & Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, California.
Lawrence Berkeley National Laboratory · USLos Alamos National Laboratory · US

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
NIGMS NIH HHS P01 GM063210NIH HHS GM063210
6 · The paper itself

Abstract

A procedure for building protein chains into maps produced by single-particle electron cryo-microscopy (cryo-EM) is described. The procedure is similar to the way an experienced structural biologist might analyze a map, focusing first on secondary structure elements such as helices and sheets, then varying the contour level to identify connections between these elements. Since the high density in a map typically follows the main-chain of the protein, the main-chain connection between secondary structure elements can often be identified as the unbranched path between them with the highest minimum value along the path. This chain-tracing procedure is then combined with finding side-chain positions based on the presence of density extending away from the main path of the chain, allowing generation of a C

Indexed as

Computational BiologyCryoelectron MicroscopyModels, MolecularProtein Interaction MappingProteinsProtein Structure, SecondarySoftwareProteinscryo-electron microscopymap interpretationmap segmentationmodel-building

Identifiers

PMID31599033
PMCPMC6933853
OpenAlexW2979414277

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.