Structures of multisubunit membrane complexes with the CRYO ARM 200-Reference-Cited by-同舟云学术

Structures of multisubunit membrane complexes with the CRYO ARM 200

Published:2022-07-21 Issue:5 Volume:71 Page:249-261
ISSN:2050-5698
Container-title:Microscopy
language:en
Short-container-title:

Author:

Gerle Christoph¹²^ORCID,Kishikawa Jun-ichi¹,Yamaguchi Tomoko³,Nakanishi Atsuko⁴⁵^ORCID,Çoruh Orkun¹⁶,Makino Fumiaki³⁷,Miyata Tomoko³,Kawamoto Akihiro¹,Yokoyama Ken⁴,Namba Keiichi³⁸⁹,Kurisu Genji¹^ORCID,Kato Takayuki¹³

Affiliation:

1. Institute for Protein Research, Osaka University , 3-2 Yamada Oka, Suita, Osaka 565-0871, Japan

2. RIKEN SPring-8 Center, Life Science Research Infrastructure Group , Sayo-gun, 1-1-1 Kouto, Sayo, Hyogo 679-5148, Japan

3. Graduate School of Frontier Biosciences, Osaka University , Suita, Japan

4. Department of Molecular Biosciences, Kyoto Sangyo University , Kamigamo-Motoyama, Kyoto 603-8555, Japan

5. Research Center for Ultra-High Voltage Electron Microscopy, Osaka University , 7-1 Mihogaoka, Ibaraki, Osaka 567-0047, Japan

6. Institute of Science and Technology Austria , Am Campus 1, Klosterneuburg, Niederösterreich 3400, Austria

7. JEOL Ltd. , 3 Chome 1-2 Musashino, Akishima, Tokyo 196-8558, Japan

8. RIKEN Center for Biosystems Dynamics Research , 1-3 Yamadaoka, Suita, Osaka 565-0871, Japan

9. JEOL YOKOGUSHI Research Alliance Laboratories, Osaka University , 1-3 Yamadaoka, Suita, Osaka 565-0871, Japan

Abstract

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.

Funder

Japan Science and Technology Agency

Japan Agency for Medical Research and Development

Japan Society for the Promotion of Science

Publisher

Oxford University Press (OUP)

Subject

Radiology, Nuclear Medicine and imaging,Instrumentation,Structural Biology

Link

https://academic.oup.com/jmicro/advance-article-pdf/doi/10.1093/jmicro/dfac037/45298369/dfac037.pdf

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