Evidence map›Paper›PMID 30144506›Full record

ArticleJournal of structural biology2018

Assessment of structural features in Cryo-EM density maps using SSE and side chain Z-scores.

Grigore Pintilie, Wah Chiu

Abstract read
In one paragraph

Article in Journal of structural biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Validation, analysis and annotation of cryo-EM structures.Acta crystallographica. Section D, Structural biology · 2021
    Article
  5. Article
  6. High resolution single particle Cryo-EM refinement using JSPR.Progress in biophysics and molecular biology · 2021
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Evolving data standards for cryo-EM structures.Structural dynamics (Melville, N.Y.) · 2020
    Article
  13. Article
  14. Cryo-EM structures ofProceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  15. Article
  16. Comparing cryo-EM structures.Journal of structural biology · 2018
    Article
  17. 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

2 authors.

Grigore PintilieDepartment of Bioengineering, Stanford University, Stanford, CA 94305, USA. Electronic address: gregp@slac.stanford.edu.
Wah ChiuDepartment of Bioengineering, Stanford University, Stanford, CA 94305, USA.

Funding

3 D ELECTRON MICROSCOPY OF MACROMOLECULES (5P41RR002250-27)P41GM103832 · NIGMS · STANFORD UNIVERSITY · PI CHIU, WAH · 2012 to 2019
$15.1M
Unified Data Resource for Large Complexes Determined by Cryo-Electron MicroscopyR01GM079429 · NIGMS · STANFORD UNIVERSITY · PI CHIU, WAH · 2007 to 2021
$11.6M
Resource for Biocomputing Visualization and InformaticsP41GM103311 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FERRIN, THOMAS E · 2012 to 2017
$8.2M
Acquisition of a 300 kV Electron Microscope for Structural BiologyS10OD021600 · OD · STANFORD UNIVERSITY · PI CHIU, WAH · 2016 to 2016
$2.0M
NIGMS NIH HHS P41 GM103311NIGMS NIH HHS P41 GM103832NIGMS NIH HHS R01 GM079429NIH HHS S10 OD021600
6 · The paper itself

Abstract

We introduce a new method for assessing resolvability of structural features in density maps from Cryo-Electron Microscopy (Cryo-EM) using fitted or derived models. It calculates Z-scores for secondary structure elements (SSEs) and side chains. Z-scores capture how much larger the cross-correlation score (CCS) is for atoms in such features at their placed locations compared to the CCS at displaced positions. Z-scores are larger when the structural features are well-resolved, as confirmed by visual analysis. This method was applied to all 66 maps submitted to the 2015/2016 EMDB map challenge. For each map, the fitted model provided by the map committee was used in this assessment. The average Z-scores for each map and fitted model correlate moderately well with reported map resolutions (r

Indexed as

Protein ConformationProtein Structure, SecondaryCryoelectron MicroscopyModels, MolecularProteasome Endopeptidase ComplexProteinsProteasome Endopeptidase ComplexProteinsCryo-Electron MicroscopyProteinsSecondary structuresSide chainsStatistics

Identifiers

PMID30144506
PMCPMC6525962

What OpenQuestion holds

Textmetadata
LicenceTDM
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.