Evidence map›Paper›PMID 35861182›Full record

ArticleMicroscopy (Oxford, England)2022

Structures of multisubunit membrane complexes with the CRYO ARM 200.

Christoph Gerle, Jun-Ichi Kishikawa, Tomoko Yamaguchi, Atsuko Nakanishi, Orkun Çoruh, Fumiaki Makino, Tomoko Miyata, Akihiro Kawamoto, Ken Yokoyama, Keiichi Namba and 2 more

Erratum issuedAbstract read
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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. An erratum has been issued. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

12 authors.

Christoph GerleInstitute for Protein Research, Osaka University, 3-2 Yamada Oka, Suita, Osaka 565-0871, Japan.ORCID 0000-0002-7265-2804
Jun-Ichi KishikawaInstitute for Protein Research, Osaka University, 3-2 Yamada Oka, Suita, Osaka 565-0871, Japan.
Tomoko YamaguchiGraduate School of Frontier Biosciences, Osaka University, Suita, Japan.
Atsuko NakanishiDepartment of Molecular Biosciences, Kyoto Sangyo University, Kamigamo-Motoyama, Kyoto 603-8555, Japan.ORCID 0000-0001-8262-0796
Orkun ÇoruhInstitute for Protein Research, Osaka University, 3-2 Yamada Oka, Suita, Osaka 565-0871, Japan.
Fumiaki MakinoGraduate School of Frontier Biosciences, Osaka University, Suita, Japan.
Tomoko MiyataGraduate School of Frontier Biosciences, Osaka University, Suita, Japan.
Akihiro KawamotoInstitute for Protein Research, Osaka University, 3-2 Yamada Oka, Suita, Osaka 565-0871, Japan.
Ken YokoyamaDepartment of Molecular Biosciences, Kyoto Sangyo University, Kamigamo-Motoyama, Kyoto 603-8555, Japan.
Keiichi NambaGraduate School of Frontier Biosciences, Osaka University, Suita, Japan.
Genji KurisuInstitute for Protein Research, Osaka University, 3-2 Yamada Oka, Suita, Osaka 565-0871, Japan.ORCID 0000-0002-5354-0807
Takayuki KatoInstitute for Protein Research, Osaka University, 3-2 Yamada Oka, Suita, Osaka 565-0871, Japan.

Funding

Japan Agency for Medical Research and Development 22ama121001j0001Japan Agency for Medical Research and Development JP16K07266Japan Agency for Medical Research and Development JP17pc0101020Japan Agency for Medical Research and Development JP19am0101117Japan Science and Technology Agency JMPMJOP1861Japan Society for the Promotion of Science 20K06514Japan Society for the Promotion of Science JP25000013
6 · The paper itself

Abstract

Progress in structural membrane biology has been significantly accelerated by the ongoing 'Resolution Revolution' in cryo-electron microscopy (cryo-EM). In particular, structure determination by single-particle analysis has evolved into the most powerful method for atomic model building of multisubunit membrane protein complexes. This has created an ever-increasing demand in cryo-EM machine time, which to satisfy is in need of new and affordable cryo-electron microscopes. Here, we review our experience in using the JEOL CRYO ARM 200 prototype for the structure determination by single-particle analysis of three different multisubunit membrane complexes: the Thermus thermophilus V-type ATPase VO complex, the Thermosynechococcus elongatus photosystem I monomer and the flagellar motor lipopolysaccharide peptidoglycan ring (LP ring) from Salmonella enterica.

Indexed as

Vacuolar Proton-Translocating ATPasesCryoelectron MicroscopyLipopolysaccharidesPeptidoglycanPhotosystem I Protein ComplexLipopolysaccharidesPeptidoglycanPhotosystem I Protein ComplexVacuolar Proton-Translocating ATPasesmolecular motorprotein structurePSItransmission electron microscopeV-ATPase

Identifiers

PMID35861182
PMCPMC9535789

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

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.