Evidence map›Paper›PMID 31217444›Full record

ArticleNature communications2019

Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex.

Diego F Gauto, Leandro F Estrozi, Charles D Schwieters, Gregory Effantin, Pavel Macek, Remy Sounier, Astrid C Sivertsen, Elena Schmidt, Rime Kerfah, Guillaume Mas and 6 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
6.6field-weighted citation impact, top 2% 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

51 citing papers in PubMed, 115 citations in OpenAlex.

  1. NMR crystallography reveals active-site protonation states of Toho-1 β-lactamase in complex with avibactam.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Review
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  4. Article
  5. AMIGO - Guided assignment ofJournal of biomolecular NMR · 2026
    Article
  6. Article
  7. AcceleratedMagnetic resonance (Gottingen, Germany) · 2026
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  9. Review
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  12. Review
  13. Article
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  15. Review
  16. IntegratingJournal of the American Chemical Society · 2024
    Article
  17. Article
  18. Review
  19. Molecular basis for curvature formation in SepF polymerization.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  20. 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

16 authors at 3 institutions in 5 countries.

Diego F GautoInstitut de Biologie Structurale (IBS), CEA, CNRS, Université Grenoble Alpes, 71, Avenue des Martyrs, F-38044, Grenoble, France.
Leandro F EstroziInstitut de Biologie Structurale (IBS), CEA, CNRS, Université Grenoble Alpes, 71, Avenue des Martyrs, F-38044, Grenoble, France. leandro.estrozi@ibs.fr.ORCID http://orcid.org/0000-0003-2548-2547
Charles D SchwietersLaboratory of Imaging Sciences, Center for Information Technology, National Institutes of Health, 12 South Drive, MSC 5624, Bethesda, MD, 20892, USA.
Gregory EffantinInstitut de Biologie Structurale (IBS), CEA, CNRS, Université Grenoble Alpes, 71, Avenue des Martyrs, F-38044, Grenoble, France.
Pavel MacekInstitut de Biologie Structurale (IBS), CEA, CNRS, Université Grenoble Alpes, 71, Avenue des Martyrs, F-38044, Grenoble, France.
Remy SounierInstitut de Biologie Structurale (IBS), CEA, CNRS, Université Grenoble Alpes, 71, Avenue des Martyrs, F-38044, Grenoble, France.
Astrid C SivertsenInstitut de Biologie Structurale (IBS), CEA, CNRS, Université Grenoble Alpes, 71, Avenue des Martyrs, F-38044, Grenoble, France.
Elena SchmidtInstitute of Biophysical Chemistry, Goethe University Frankfurt am Main, 60438 Frankfurt am Main, Germany.
Rime KerfahInstitut de Biologie Structurale (IBS), CEA, CNRS, Université Grenoble Alpes, 71, Avenue des Martyrs, F-38044, Grenoble, France.
Guillaume MasInstitut de Biologie Structurale (IBS), CEA, CNRS, Université Grenoble Alpes, 71, Avenue des Martyrs, F-38044, Grenoble, France.
Jacques-Philippe ColletierInstitut de Biologie Structurale (IBS), CEA, CNRS, Université Grenoble Alpes, 71, Avenue des Martyrs, F-38044, Grenoble, France.
Peter GüntertInstitute of Biophysical Chemistry, Goethe University Frankfurt am Main, 60438 Frankfurt am Main, Germany.ORCID http://orcid.org/0000-0002-2911-7574
Adrien FavierInstitut de Biologie Structurale (IBS), CEA, CNRS, Université Grenoble Alpes, 71, Avenue des Martyrs, F-38044, Grenoble, France. adrien.favier@ibs.fr.ORCID http://orcid.org/0000-0003-2511-2300
Guy SchoehnInstitut de Biologie Structurale (IBS), CEA, CNRS, Université Grenoble Alpes, 71, Avenue des Martyrs, F-38044, Grenoble, France.ORCID http://orcid.org/0000-0002-1459-3201
Paul SchandaInstitut de Biologie Structurale (IBS), CEA, CNRS, Université Grenoble Alpes, 71, Avenue des Martyrs, F-38044, Grenoble, France. paul.schanda@ibs.fr.ORCID http://orcid.org/0000-0002-9350-7606
Jerome BoisbouvierInstitut de Biologie Structurale (IBS), CEA, CNRS, Université Grenoble Alpes, 71, Avenue des Martyrs, F-38044, Grenoble, France.ORCID http://orcid.org/0000-0003-3278-3639
Centre National de la Recherche Scientifique · FRGoethe University Frankfurt · DENational Institutes of Health · US

Funding

Agence Nationale de la Recherche (French National Research Agency) ANR-10-PDOC-011-01EC | EC Seventh Framework Programm | FP7 Ideas: European Research Council (FP7-IDEAS-ERC - Specific Programme: "Ideas" Implementing the Seventh Framework Programme of the European Community for Research, Technological Development and Demonstration Activities (2007 to 2013)) CoG-260887EC | EC Seventh Framework Programm | FP7 Ideas: European Research Council (FP7-IDEAS-ERC - Specific Programme: "Ideas" Implementing the Seventh Framework Programme of the European Community for Research, Technological Development and Demonstration Activities (2007 to 2013)) StG-311318
6 · The paper itself

Abstract

Atomic-resolution structure determination is crucial for understanding protein function. Cryo-EM and NMR spectroscopy both provide structural information, but currently cryo-EM does not routinely give access to atomic-level structural data, and, generally, NMR structure determination is restricted to small (<30 kDa) proteins. We introduce an integrated structure determination approach that simultaneously uses NMR and EM data to overcome the limits of each of these methods. The approach enables structure determination of the 468 kDa large dodecameric aminopeptidase TET2 to a precision and accuracy below 1 Å by combining secondary-structure information obtained from near-complete magic-angle-spinning NMR assignments of the 39 kDa-large subunits, distance restraints from backbone amides and ILV methyl groups, and a 4.1 Å resolution EM map. The resulting structure exceeds current standards of NMR and EM structure determination in terms of molecular weight and precision. Importantly, the approach is successful even in cases where only medium-resolution cryo-EM data are available.

Indexed as

Protein Structure, QuaternaryAminopeptidasesBacterial ProteinsCryoelectron MicroscopyMagnetic Resonance SpectroscopyMolecular Dynamics SimulationMolecular WeightMultienzyme ComplexesPyrococcus horikoshiiAminopeptidasesBacterial ProteinsMultienzyme Complexes

Identifiers

PMID31217444
PMCPMC6584647
OpenAlexW2950508986

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.