Evidence map›Paper›PMID 24569482›Full record

ArticleeLife2014

Atomic model of the F420-reducing [NiFe] hydrogenase by electron cryo-microscopy using a direct electron detector.

Matteo Allegretti, Deryck J Mills, Greg McMullan, Werner Kühlbrandt, Janet Vonck

Open access · goldAbstract readVideo-Audio Media
In one paragraph

Article in eLife, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.

0numbers the graph read from it
0cells of the map it votes in
77citing papers in PubMed
10.1field-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

77 citing papers in PubMed, 140 citations in OpenAlex.

  1. Article
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  3. Cryo-EM single-particle analysis expanding towards increasingly native samples.Acta crystallographica. Section D, Structural biology · 2025
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  7. NADPApplied and environmental microbiology · 2023
    Article
  8. Article
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  10. Article
  11. Article
  12. Article
  13. Article
  14. Forty years in cryoEM of membrane proteins.Microscopy (Oxford, England) · 2022
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Development of imaging scaffolds for cryo-electron microscopy.Current opinion in structural biology · 2020
    Review

17 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 2 institutions in 2 countries.

Matteo AllegrettiDepartment of Structural Biology, Max Planck Institute of Biophysics, Frankfurt, Germany.
Deryck J Mills
Greg McMullan
Werner Kühlbrandt
Janet Vonck
Max Planck Institute of Biophysics · DEMRC Laboratory of Molecular Biology · GB

Funding

Medical Research Council MC_U105184322
6 · The paper itself

Abstract

The introduction of direct electron detectors with higher detective quantum efficiency and fast read-out marks the beginning of a new era in electron cryo-microscopy. Using the FEI Falcon II direct electron detector in video mode, we have reconstructed a map at 3.36 Å resolution of the 1.2 MDa F420-reducing hydrogenase (Frh) from methanogenic archaea from only 320,000 asymmetric units. Videos frames were aligned by a combination of image and particle alignment procedures to overcome the effects of beam-induced motion. The reconstructed density map shows all secondary structure as well as clear side chain densities for most residues. The full coordination of all cofactors in the electron transfer chain (a [NiFe] center, four [4Fe4S] clusters and an FAD) is clearly visible along with a well-defined substrate access channel. From the rigidity of the complex we conclude that catalysis is diffusion-limited and does not depend on protein flexibility or conformational changes. DOI: http://dx.doi.org/10.7554/eLife.01963.001.

Indexed as

Models, MolecularAmino Acid SequenceArchaeal ProteinsCatalysisCryoelectron MicroscopyElectronsEquipment DesignFourier AnalysisImage Processing, Computer-AssistedMethanobacteriaceaeMolecular Sequence DataOxidoreductasesProtein Structure, SecondaryStructure-Activity RelationshipVideo RecordingArchaeal Proteinscoenzyme F420 hydrogenaseOxidoreductasescryo-electron microscopymethanogenesisMethanothermobacter marburgensis[NiFe] hydrogenase

Identifiers

PMID24569482
PMCPMC3930138
OpenAlexW2098913646

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.