Evidence map›Paper›PMID 25760083›Full record

ArticleeLife2015

2.8 Å resolution reconstruction of the Thermoplasma acidophilum 20S proteasome using cryo-electron microscopy.

Melody G Campbell, David Veesler, Anchi Cheng, Clinton S Potter, Bridget Carragher

Open access · goldAbstract read
In one paragraph

Article in eLife, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 98 papers.

0numbers the graph read from it
0cells of the map it votes in
98citing papers in PubMed
44.7field-weighted citation impact, top 1% of its field
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

98 citing papers in PubMed, 184 citations in OpenAlex.

  1. Article
  2. AlignPCA-2D: PCA-reduced Euclidean vector alignment for 2D classification in cryo-EM.Acta crystallographica. Section D, Structural biology · 2026
    Article
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  4. Review
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  9. Factors affecting macromolecule orientations in thin films formed in cryo-EM.Acta crystallographica. Section D, Structural biology · 2024
    Article
  10. Article
  11. Cryo-EM for Small Molecules.Current protocols · 2022
    Review
  12. Article
  13. Article
  14. Review
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  17. Article
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  20. Article

38 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

5 authors at 3 institutions in 1 country.

Melody G CampbellNational Resource for Automated Molecular Microscopy, The Scripps Research Institute, La Jolla, United States.
David VeeslerNational Resource for Automated Molecular Microscopy, The Scripps Research Institute, La Jolla, United States.
Anchi ChengNational Resource for Automated Molecular Microscopy, The Scripps Research Institute, La Jolla, United States.
Clinton S PotterNational Resource for Automated Molecular Microscopy, The Scripps Research Institute, La Jolla, United States.
Bridget CarragherNational Resource for Automated Molecular Microscopy, The Scripps Research Institute, La Jolla, United States.
New York Structural Biology Center · USScripps Research Institute · USSeattle University · US

Funding

TRD #3: An automated and streamlined pipeline for in-situ molecular microscopyP41GM103310 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI DE MARCO, ALEX, KIEFT, JEFFREY S · 2012 to 2021
$14.7M
NIGMS NIH HHS GM103310NIGMS NIH HHS P41 GM103310
6 · The paper itself

Abstract

Recent developments in detector hardware and image-processing software have revolutionized single particle cryo-electron microscopy (cryoEM) and led to a wave of near-atomic resolution (typically ∼3.3 Å) reconstructions. Reaching resolutions higher than 3 Å is a prerequisite for structure-based drug design and for cryoEM to become widely interesting to pharmaceutical industries. We report here the structure of the 700 kDa Thermoplasma acidophilum 20S proteasome (T20S), determined at 2.8 Å resolution by single-particle cryoEM. The quality of the reconstruction enables identifying the rotameric conformation adopted by some amino-acid side chains (rotamers) and resolving ordered water molecules, in agreement with the expectations for crystal structures at similar resolutions. The results described in this manuscript demonstrate that single particle cryoEM is capable of competing with X-ray crystallography for determination of protein structures of suitable quality for rational drug design.

Indexed as

Archaeal ProteinsCryoelectron MicroscopyCrystallography, X-RayImaging, Three-DimensionalModels, MolecularProteasome Endopeptidase ComplexProtein ConformationReproducibility of ResultsThermoplasmaArchaeal ProteinsProteasome Endopeptidase Complexbiophysicsdirect detectorselectron microscopyimage processingstructural biologyT. acidophilum

Identifiers

PMID25760083
PMCPMC4391500
OpenAlexW2143205611

What OpenQuestion holds

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LicenceCC BY
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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.