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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.
Afiliación
  • Gerle C; Institute for Protein Research, Osaka University, 3-2 Yamada Oka, Suita, Osaka 565-0871, Japan.
  • Kishikawa JI; RIKEN SPring-8 Center, Life Science Research Infrastructure Group, Sayo-gun, 1-1-1 Kouto, Sayo, Hyogo 679-5148, Japan.
  • Yamaguchi T; Institute for Protein Research, Osaka University, 3-2 Yamada Oka, Suita, Osaka 565-0871, Japan.
  • Nakanishi A; Graduate School of Frontier Biosciences, Osaka University, Suita, Japan.
  • Çoruh O; Department of Molecular Biosciences, Kyoto Sangyo University, Kamigamo-Motoyama, Kyoto 603-8555, Japan.
  • Makino F; Research Center for Ultra-High Voltage Electron Microscopy, Osaka University, 7-1 Mihogaoka, Ibaraki, Osaka 567-0047, Japan.
  • Miyata T; Institute for Protein Research, Osaka University, 3-2 Yamada Oka, Suita, Osaka 565-0871, Japan.
  • Kawamoto A; Institute of Science and Technology Austria, Am Campus 1, Klosterneuburg, Niederösterreich 3400, Austria.
  • Yokoyama K; Graduate School of Frontier Biosciences, Osaka University, Suita, Japan.
  • Namba K; JEOL Ltd., 3 Chome 1-2 Musashino, Akishima, Tokyo 196-8558, Japan.
  • Kurisu G; Graduate School of Frontier Biosciences, Osaka University, Suita, Japan.
  • Kato T; Institute for Protein Research, Osaka University, 3-2 Yamada Oka, Suita, Osaka 565-0871, Japan.
Microscopy (Oxf) ; 71(5): 249-261, 2022 Oct 06.
Article en En | MEDLINE | ID: mdl-35861182
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.
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Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: ATPasas de Translocación de Protón Vacuolares Idioma: En Revista: Microscopy (Oxf) Año: 2022 Tipo del documento: Article País de afiliación: Japón

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: ATPasas de Translocación de Protón Vacuolares Idioma: En Revista: Microscopy (Oxf) Año: 2022 Tipo del documento: Article País de afiliación: Japón