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...

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Detalles Bibliográficos
Autores principales: 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
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2022
Materias:
Review
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
Descripción
Sumario: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.

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