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Structures of multisubunit membrane complexes with the CRYO ARM 200
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 multisubu...
Autores principales: | , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9535789/ https://www.ncbi.nlm.nih.gov/pubmed/35861182 http://dx.doi.org/10.1093/jmicro/dfac037 |
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author | Gerle, Christoph Kishikawa, Jun-ichi Yamaguchi, Tomoko Nakanishi, Atsuko Çoruh, Orkun Makino, Fumiaki Miyata, Tomoko Kawamoto, Akihiro Yokoyama, Ken Namba, Keiichi Kurisu, Genji Kato, Takayuki |
author_facet | Gerle, Christoph Kishikawa, Jun-ichi Yamaguchi, Tomoko Nakanishi, Atsuko Çoruh, Orkun Makino, Fumiaki Miyata, Tomoko Kawamoto, Akihiro Yokoyama, Ken Namba, Keiichi Kurisu, Genji Kato, Takayuki |
author_sort | Gerle, Christoph |
collection | PubMed |
description | 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 V(O) complex, the Thermosynechococcus elongatus photosystem I monomer and the flagellar motor lipopolysaccharide peptidoglycan ring (LP ring) from Salmonella enterica. |
format | Online Article Text |
id | pubmed-9535789 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-95357892022-10-07 Structures of multisubunit membrane complexes with the CRYO ARM 200 Gerle, Christoph Kishikawa, Jun-ichi Yamaguchi, Tomoko Nakanishi, Atsuko Çoruh, Orkun Makino, Fumiaki Miyata, Tomoko Kawamoto, Akihiro Yokoyama, Ken Namba, Keiichi Kurisu, Genji Kato, Takayuki Microscopy (Oxf) Review 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 V(O) complex, the Thermosynechococcus elongatus photosystem I monomer and the flagellar motor lipopolysaccharide peptidoglycan ring (LP ring) from Salmonella enterica. Oxford University Press 2022-07-21 /pmc/articles/PMC9535789/ /pubmed/35861182 http://dx.doi.org/10.1093/jmicro/dfac037 Text en © The Author(s) 2022. Published by Oxford University Press on behalf of The Japanese Society of Microscopy. https://creativecommons.org/licenses/by/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Review Gerle, Christoph Kishikawa, Jun-ichi Yamaguchi, Tomoko Nakanishi, Atsuko Çoruh, Orkun Makino, Fumiaki Miyata, Tomoko Kawamoto, Akihiro Yokoyama, Ken Namba, Keiichi Kurisu, Genji Kato, Takayuki Structures of multisubunit membrane complexes with the CRYO ARM 200 |
title | Structures of multisubunit membrane complexes with the CRYO ARM 200 |
title_full | Structures of multisubunit membrane complexes with the CRYO ARM 200 |
title_fullStr | Structures of multisubunit membrane complexes with the CRYO ARM 200 |
title_full_unstemmed | Structures of multisubunit membrane complexes with the CRYO ARM 200 |
title_short | Structures of multisubunit membrane complexes with the CRYO ARM 200 |
title_sort | structures of multisubunit membrane complexes with the cryo arm 200 |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9535789/ https://www.ncbi.nlm.nih.gov/pubmed/35861182 http://dx.doi.org/10.1093/jmicro/dfac037 |
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