Structures of multisubunit membrane complexes with the CRYO ARM 200

Microscopy (Oxf). 2022 Oct 6;71(5):249-261. doi: 10.1093/jmicro/dfac037.

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.

Keywords: PSI; V-ATPase; molecular motor; protein structure; transmission electron microscope.

MeSH terms

  • Cryoelectron Microscopy / methods
  • Lipopolysaccharides
  • Peptidoglycan
  • Photosystem I Protein Complex / metabolism
  • Vacuolar Proton-Translocating ATPases* / chemistry
  • Vacuolar Proton-Translocating ATPases* / metabolism

Substances

  • Lipopolysaccharides
  • Peptidoglycan
  • Photosystem I Protein Complex
  • Vacuolar Proton-Translocating ATPases