Evidence map›Paper›PMID 32733087›Full record

ReviewCommunications biology2020

Opportunities and challenges for assigning cofactors in cryo-EM density maps of chlorophyll-containing proteins.

Christopher J Gisriel, Jimin Wang, Gary W Brudvig, Donald A Bryant

Abstract readReview
In one paragraph

Review in Communications biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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

22 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Modified chlorophyll pigment at ChlChemical science · 2025
    Article
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  7. Article
  8. Review
  9. Article
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  18. Review
  19. Article
  20. Identification of MgActa crystallographica. Section D, Structural biology · 2021
    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.

Christopher J GisrielDepartment of Chemistry, Yale University, New Haven, CT, 06520, USA. christopher.gisriel@yale.edu.ORCID http://orcid.org/0000-0002-8011-0052
Jimin WangDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, 06520, USA.ORCID http://orcid.org/0000-0002-4504-8038
Gary W BrudvigDepartment of Chemistry, Yale University, New Haven, CT, 06520, USA.ORCID http://orcid.org/0000-0002-7040-1892
Donald A BryantDepartment of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA, 16802, USA.ORCID http://orcid.org/0000-0003-2782-5988

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The accurate assignment of cofactors in cryo-electron microscopy maps is crucial in determining protein function. This is particularly true for chlorophylls (Chls), for which small structural differences lead to important functional differences. Recent cryo-electron microscopy structures of Chl-containing protein complexes exemplify the difficulties in distinguishing Chl b and Chl f from Chl a. We use these structures as examples to discuss general issues arising from local resolution differences, properties of electrostatic potential maps, and the chemical environment which must be considered to make accurate assignments. We offer suggestions for how to improve the reliability of such assignments.

Indexed as

Cryoelectron MicroscopyChlorophyllChlorophyll Binding ProteinsModels, MolecularChlorophyllChlorophyll Binding Proteins

Identifiers

PMID32733087
PMCPMC7393486

What OpenQuestion holds

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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.