Evidence map›Paper›PMID 35275189›Full record

ArticleMicroscopy (Oxford, England)2022

Interaction of human erythrocyte catalase with air-water interface in cryoEM.

Shaoxia Chen, Jade Li, Kutti R Vinothkumar, Richard Henderson

Open access · hybridAbstract read
In one paragraph

Article in Microscopy (Oxford, England), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

21 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Foam film vitrification for cryo-EM.Nature communications · 2025
    Article
  9. Article
  10. Article
  11. Article
  12. Factors affecting macromolecule orientations in thin films formed in cryo-EM.Acta crystallographica. Section D, Structural biology · 2024
    Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Cryo-electron microscopy-based drug design.Frontiers in molecular biosciences · 2024
    Review
  18. Structure determination by cryoEM at 100 keV.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  19. 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

4 authors at 2 institutions in 2 countries.

Shaoxia ChenMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.
Jade LiMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.
Kutti R VinothkumarMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.
Richard HendersonMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.ORCID 0000-0003-1444-0528
MRC Laboratory of Molecular Biology · GBTata Institute of Fundamental Research · IN

Funding

Medical Research Council MC_U105184322Medical Research Council MC_U105184326
6 · The paper itself

Abstract

One of the key goals in single-particle cryo-microscopy is to obtain a uniform distribution of particle orientations, so that the three-dimensional structure has isotropic resolution in Fourier space. A common problem arises from the interaction of protein molecules with the air-water interface that exists on both surfaces of the thin film of liquid that is formed prior to plunge-freezing into liquid ethane. Some proteins and other macromolecular complexes are disrupted by interaction with the air-water interface. Other proteins or macromolecules either become concentrated through their interaction with the interface or are excluded because they bind strongly to some other part of the grid or the filter paper used in blotting. In this paper, the interaction of human erythrocyte catalase with the air-water interface is investigated and minimized by the addition of certain detergents. Detergents can form an amphipathic monolayer at the air-water interface that creates a barrier and leaves the molecules free to adopt a variety of orientations, thus facilitating the 3D structure determination. These results suggest that further characterization and development of detergents for cryo-microscopy plunge-freezing would be useful.

Indexed as

ProteinsWaterCatalaseCryoelectron MicroscopyErythrocytesHumansCatalaseProteinsWater3D structureair–water interfaceCHAPSO detergentcryoEMhuman erythrocyte catalase

Identifiers

PMID35275189
PMCPMC8855524
OpenAlexW4213267416

What OpenQuestion holds

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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.