Evidence map›Paper›PMID 25982529›Full record

ArticleStructure (London, England : 1993)2015

Efficient estimation of three-dimensional covariance and its application in the analysis of heterogeneous samples in cryo-electron microscopy.

Hstau Y Liao, Yaser Hashem, Joachim Frank

Abstract read
In one paragraph

Article in Structure (London, England : 1993), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Principal component analysis is limited to low-resolution analysis in cryoEM.Acta crystallographica. Section D, Structural biology · 2021
    Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. Structural Variability from Noisy Tomographic Projections.SIAM journal on imaging sciences · 2018
    Article
  14. Article
  15. 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.

Hstau Y LiaoDepartment of Biochemistry and Molecular Biophysics, Columbia University, 650 West 168 Street, New York, NY 10032, USA.
Yaser HashemArchitecture et Réactivité de l'ARN, Institut de Biologie Moléculaire et Cellulaire, CNRS, Université de Strasbourg, 15 Rue René Descartes, 67084 Strasbourg, France.
Joachim FrankDepartment of Biochemistry and Molecular Biophysics, Columbia University, 650 West 168 Street, New York, NY 10032, USA; Department of Biological Sciences, Columbia University, 600 Fairchild Center, New York, NY 10027, USA; Department of Biochemistry and Molecular Biophysics, Howard Hughes Medical Institute, Columbia University, 650 West 168 Street, New York, NY 10032, USA. Electronic address: jf2192@cumc.columbia.edu.

Funding

STRUCTURE ANALYSIS OF MACROMOLECULAR ASSEMBLIESR01GM029169 · NIGMS · WADSWORTH CENTER · PI FRANK, JOACHIM · 1985 to 2019
$6.1M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM029169NIGMS NIH HHS R01 GM29169
6 · The paper itself

Abstract

Single-particle cryogenic electron microscopy (cryo-EM) is a powerful tool for the study of macromolecular structures at high resolution. Classification allows multiple structural states to be extracted and reconstructed from the same sample. One classification approach is via the covariance matrix, which captures the correlation between every pair of voxels. Earlier approaches employ computing-intensive resampling and estimate only the eigenvectors of the matrix, which are then used in a separate fast classification step. We propose an iterative scheme to explicitly estimate the covariance matrix in its entirety. In our approach, the flexibility in choosing the solution domain allows us to examine a part of the molecule in greater detail. Three-dimensional covariance maps obtained in this way from experimental data (cryo-EM images of the eukaryotic pre-initiation complex) prove to be in excellent agreement with conclusions derived by using traditional approaches, revealing in addition the interdependencies of ligand bindings and structural changes.

Indexed as

Models, MolecularAnalysis of VarianceCryoelectron MicroscopyData Interpretation, StatisticalRibosome Subunits

Identifiers

PMID25982529
PMCPMC4456258

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.