Evidence map›Paper›PMID 33753866›Full record

ArticleCommunications biology2021

High-resolution cryo-EM structure of photosystem II reveals damage from high-dose electron beams.

Koji Kato, Naoyuki Miyazaki, Tasuku Hamaguchi, Yoshiki Nakajima, Fusamichi Akita, Koji Yonekura, Jian-Ren Shen

Abstract read
In one paragraph

Article in Communications biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing 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

41 citing papers in PubMed.

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  3. Biophysical journal · 2026
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  10. Cryo-EM meets crystallography: A model-independent view of the heteronuclear MnProceedings of the National Academy of Sciences of the United States of America · 2025
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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

7 authors.

Koji Kato *Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University, Okayama, Japan.
Naoyuki Miyazaki *Life Science Center for Survival Dynamics, Tsukuba Advanced Research Alliance (TARA), University of Tsukuba, Ibaraki, Japan.ORCID 0000-0002-4880-7300
Tasuku Hamaguchi *Biostructural Mechanism Laboratory, RIKEN Spring-8 Center, Hyogo, Japan.ORCID 0000-0003-0876-7700
Yoshiki NakajimaResearch Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University, Okayama, Japan.ORCID 0000-0002-0529-8075
Fusamichi AkitaResearch Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University, Okayama, Japan. fusamichi_a@okayama-u.ac.jp.ORCID 0000-0003-0537-6157
Koji YonekuraBiostructural Mechanism Laboratory, RIKEN Spring-8 Center, Hyogo, Japan. yone@spring8.or.jp.ORCID 0000-0001-5520-4391
Jian-Ren ShenResearch Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University, Okayama, Japan. shen@cc.okayama-u.ac.jp.ORCID 0000-0003-4471-8797

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Photosystem II (PSII) plays a key role in water-splitting and oxygen evolution. X-ray crystallography has revealed its atomic structure and some intermediate structures. However, these structures are in the crystalline state and its final state structure has not been solved. Here we analyzed the structure of PSII in solution at 1.95 Å resolution by single-particle cryo-electron microscopy (cryo-EM). The structure obtained is similar to the crystal structure, but a PsbY subunit was visible in the cryo-EM structure, indicating that it represents its physiological state more closely. Electron beam damage was observed at a high-dose in the regions that were easily affected by redox states, and reducing the beam dosage by reducing frames from 50 to 2 yielded a similar resolution but reduced the damage remarkably. This study will serve as a good indicator for determining damage-free cryo-EM structures of not only PSII but also all biological samples, especially redox-active metalloproteins.

Indexed as

Cryoelectron MicroscopyBacterial ProteinsElectronsModels, MolecularOxidation-ReductionPhotosystem II Protein ComplexProtein ConformationThermosynechococcusBacterial ProteinsPhotosystem II Protein Complex

Identifiers

PMID33753866
PMCPMC7985191

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Registered trials

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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.