Evidence map›Paper›PMID 25910204›Full record

ReviewCell2015

A primer to single-particle cryo-electron microscopy.

Yifan Cheng, Nikolaus Grigorieff, Pawel A Penczek, Thomas Walz

Abstract readReview
In one paragraph

Review in Cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 270 papers.

0numbers the graph read from it
0cells of the map it votes in
270citing 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

270 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Visual exoproteomics ofbioRxiv : the preprint server for biology · 2026
    Article
  5. A DNN Biophysics Model with Topological and Electrostatic Features.Journal of chemical information and modeling · 2026
    Article
  6. Critical evaluation of two neutron structures of Mn superoxide dismutase with quantum refinement.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2026
    Article
  7. Review
  8. Review
  9. Review
  10. Review
  11. Review
  12. Article
  13. Article
  14. Cryogenic light microscopy of vitrified samples with angstrom precision.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Article
  20. Article

210 more citing papers are in PubMed but not listed here.

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.

Yifan ChengDepartment of Biochemistry and Biophysics, University of California, San Francisco, CA 94158, USA.
Nikolaus GrigorieffJanelia Research Campus, 19700 Helix Drive, Ashburn, VA 20147, USA.
Pawel A PenczekDepartment of Biochemistry and Molecular Biology, The University of Texas-Houston Medical School, 6431 Fannin Street, MSB 6.220, Houston, TX 77030, USA.
Thomas WalzDepartment of Cell Biology and Howard Hughes Medical Institute, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA. Electronic address: twalz@hms.harvard.edu.

Funding

X-ray Screening and Rapid Structure DeterminationP50GM082250 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FRANKEL, ALAN D · 2007 to 2018
$48.8M
Single particle reconstructionP01GM062580 · NIGMS · HARVARD MEDICAL SCHOOL · PI HARRISON, STEPHEN COPLAN · 2001 to 2016
$23.7M
HIGH RESOLUTION IN SINGLE PARTICLE RECONSTRUCTIONR01GM060635 · NIGMS · WADSWORTH CENTER · PI PENCZEK, PAWEL A. · 2000 to 2016
$4.3M
Mechanism of gate-opening in the 20S proteasome induced by the proteasomal ATPaseR01GM082893 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI CHENG, YIFAN · 2008 to 2017
$2.8M
Structures and gating mechanisms of TRP ion channelsR01GM098672 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI CHENG, YIFAN · 2011 to 2018
$2.6M
Howard Hughes Medical InstituteNIGMS NIH HHS P01 GM062580NIGMS NIH HHS P50 GM082250NIGMS NIH HHS R01 GM060635NIGMS NIH HHS R01 GM082893NIGMS NIH HHS R01 GM098672NIGMS NIH HHS R01 GM60635
6 · The paper itself

Abstract

Cryo-electron microscopy (cryo-EM) of single-particle specimens is used to determine the structure of proteins and macromolecular complexes without the need for crystals. Recent advances in detector technology and software algorithms now allow images of unprecedented quality to be recorded and structures to be determined at near-atomic resolution. However, compared with X-ray crystallography, cryo-EM is a young technique with distinct challenges. This primer explains the different steps and considerations involved in structure determination by single-particle cryo-EM to provide an overview for scientists wishing to understand more about this technique and the interpretation of data obtained with it, as well as a starting guide for new practitioners.

Indexed as

Molecular ConformationAlgorithmsCryoelectron MicroscopyImage Processing, Computer-AssistedModels, MolecularProtein ConformationProteinsProteins

Identifiers

PMID25910204
PMCPMC4409659

What OpenQuestion holds

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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.