Evidence map›Paper›PMID 28867613›Full record

ArticleStructure (London, England : 1993)2017

High-Resolution Cryo-EM Maps and Models: A Crystallographer's Perspective.

Alexander Wlodawer, Mi Li, Zbigniew Dauter

Abstract read
In one paragraph

Article in Structure (London, England : 1993), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing 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

35 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
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  11. Article
  12. Validation, analysis and annotation of cryo-EM structures.Acta crystallographica. Section D, Structural biology · 2021
    Article
  13. Vagabond: bond-based parametrization reduces overfitting for refinement of proteins.Acta crystallographica. Section D, Structural biology · 2021
    Article
  14. Article
  15. The accuracy of protein models automatically built into cryo-EM maps with ARP/wARP.Acta crystallographica. Section D, Structural biology · 2021
    Article
  16. Combine Cryo-EM Density Map and Residue Contact for Protein Structure Prediction - A Case Study.ACM-BCB ... ... : the ... ACM Conference on Bioinformatics, Computational Biology and Biomedicine. ACM Conference on Bioinformatics, Computational Biology and Biomedicine · 2020
    Article
  17. Article
  18. Refinement of organic crystal structures with multipolar electron scattering factors.Acta crystallographica. Section A, Foundations and advances · 2020
    Article
  19. Article
  20. 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

3 authors.

Alexander WlodawerProtein Structure Section, Macromolecular Crystallography Laboratory, National Cancer Institute, Frederick, MD 21702, USA. Electronic address: wlodawer@nih.gov.
Mi LiProtein Structure Section, Macromolecular Crystallography Laboratory, National Cancer Institute, Frederick, MD 21702, USA; Basic Science Program, Leidos Biomedical Research, Frederick National Laboratory for Cancer Research, Frederick, MD 21702, USA.
Zbigniew DauterSynchrotron Radiation Research Section, Macromolecular Crystallography Laboratory, NCI, Argonne National Laboratory, Argonne, IL 60439, USA.

Funding

Protein StructureZIABC010348 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI WLODAWER, ALEXANDER · 2009 to 2025
$27.5M
Macromolecular Crystallography Research with Synchrotron RadiationZIABC010378 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI DAUTER, ZBIGNIEW · 2009 to 2020
$18.8M
CCR NIH HHS HHSN261200800001CIntramural NIH HHS ZIA BC010348NCI NIH HHS HHSN261200800001E
6 · The paper itself

Abstract

The appearance of ten high-resolution cryoelectron microscopy (cryo-EM) maps of proteins, ribosomes, and viruses was compared with the experimentally phased crystallographic electron density maps of four proteins. We found that maps calculated at a similar resolution by the two techniques are quite comparable in their appearance, although cryo-EM maps, even when sharpened, seem to be a little less detailed. An analysis of models fitted to the cryo-EM maps indicated the presence of significant problems in almost all of them, including incorrect geometry, clashes between atoms, and discrepancies between the map density and the fitted models. In particular, the treatment of the atomic displacement (B) factors was meaningless in almost all analyzed cryo-EM models. Stricter cryo-EM structure deposition standards and their better enforcement are needed.

Indexed as

Cryoelectron MicroscopyCrystallography, X-RayModels, MolecularProtein ConformationProteinsRibosomesVirusesProteinscryoelectron microscopyelectron densityresolutionstructure quality

Identifiers

PMID28867613
PMCPMC5657611

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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.