Evidence map›Paper›PMID 38734767›Full record

ArticleNature communications2024

High-confidence 3D template matching for cryo-electron tomography.

Sergio Cruz-León, Tomáš Majtner, Patrick C Hoffmann, Jan Philipp Kreysing, Sebastian Kehl, Maarten W Tuijtel, Stefan L Schaefer, Katharina Geißler, Martin Beck, Beata Turoňová and 1 more

Abstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing 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

44 citing papers in PubMed.

  1. Review
  2. Visualization of membrane-stabilized SorCS2Journal of structural biology: X · 2026
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  7. CoCryoViS: Collaborative online cryo-electron tomography visualization system.Protein science : a publication of the Protein Society · 2026
    Article
  8. Review
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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

11 authors.

Sergio Cruz-LeónDepartment of Theoretical Biophysics, Max Planck Institute of Biophysics, Max-von-Laue-Str. 3, 60438, Frankfurt am Main, Germany.ORCID http://orcid.org/0000-0003-1256-2206
Tomáš MajtnerDepartment of Molecular Sociology, Max Planck Institute of Biophysics, Max-von-Laue-Str. 3, 60438, Frankfurt am Main, Germany.ORCID http://orcid.org/0000-0002-5279-8806
Patrick C HoffmannDepartment of Molecular Sociology, Max Planck Institute of Biophysics, Max-von-Laue-Str. 3, 60438, Frankfurt am Main, Germany.ORCID http://orcid.org/0000-0003-3421-6363
Jan Philipp KreysingDepartment of Molecular Sociology, Max Planck Institute of Biophysics, Max-von-Laue-Str. 3, 60438, Frankfurt am Main, Germany.ORCID http://orcid.org/0000-0002-4770-6313
Sebastian KehlMax Planck Computing and Data Facility, Gießenbachstraße 2, 85748, Garching, Germany.ORCID http://orcid.org/0000-0002-4143-9859
Maarten W TuijtelDepartment of Molecular Sociology, Max Planck Institute of Biophysics, Max-von-Laue-Str. 3, 60438, Frankfurt am Main, Germany.ORCID http://orcid.org/0000-0002-0615-572X
Stefan L SchaeferDepartment of Theoretical Biophysics, Max Planck Institute of Biophysics, Max-von-Laue-Str. 3, 60438, Frankfurt am Main, Germany.ORCID http://orcid.org/0000-0001-7942-8701
Katharina GeißlerDepartment of Molecular Sociology, Max Planck Institute of Biophysics, Max-von-Laue-Str. 3, 60438, Frankfurt am Main, Germany.ORCID http://orcid.org/0009-0000-7875-7052
Martin BeckDepartment of Molecular Sociology, Max Planck Institute of Biophysics, Max-von-Laue-Str. 3, 60438, Frankfurt am Main, Germany. martin.beck@biophys.mpg.de.ORCID http://orcid.org/0000-0002-7397-1321
Beata TuroňováDepartment of Molecular Sociology, Max Planck Institute of Biophysics, Max-von-Laue-Str. 3, 60438, Frankfurt am Main, Germany. beata.turonova@biophys.mpg.de.ORCID http://orcid.org/0000-0002-5457-4478
Gerhard HummerDepartment of Theoretical Biophysics, Max Planck Institute of Biophysics, Max-von-Laue-Str. 3, 60438, Frankfurt am Main, Germany. gerhard.hummer@biophys.mpg.de.ORCID http://orcid.org/0000-0001-7768-746X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Visual proteomics attempts to build atlases of the molecular content of cells but the automated annotation of cryo electron tomograms remains challenging. Template matching (TM) and methods based on machine learning detect structural signatures of macromolecules. However, their applicability remains limited in terms of both the abundance and size of the molecular targets. Here we show that the performance of TM is greatly improved by using template-specific search parameter optimization and by including higher-resolution information. We establish a TM pipeline with systematically tuned parameters for the automated, objective and comprehensive identification of structures with confidence 10 to 100-fold above the noise level. We demonstrate high-fidelity and high-confidence localizations of nuclear pore complexes, vaults, ribosomes, proteasomes, fatty acid synthases, lipid membranes and microtubules, and individual subunits inside crowded eukaryotic cells. We provide software tools for the generic implementation of our method that is broadly applicable towards realizing visual proteomics.

Indexed as

Cryoelectron MicroscopyElectron Microscope TomographyProteasome Endopeptidase ComplexProteomicsRibosomesSoftwareAlgorithmsFatty Acid SynthasesHumansImage Processing, Computer-AssistedImaging, Three-DimensionalMachine LearningMicrotubulesNuclear PoreFatty Acid SynthasesProteasome Endopeptidase Complex

Identifiers

PMID38734767
PMCPMC11088655

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.