The stalk connecting the F1 and F0 domains of ATP synthase visualized by electron microscopy of unstained specimens

E. coli F1 F0 ATP synthase has been reconstituted into membranes and visualized by electron microscopy of unstained samples preserved in thin layers of amorphous ice. Unlike previous observations in negative stain, these specimens are not exposed to potentially denaturing or perturbing conditions, h...

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Bibliographic Details
Published in:FEBS letters 1987-07, Vol.219 (2), p.274-278
Main Authors: Gogol, Edward P., Lücken, Uwe, Capaldi, Roderick A.
Format: Article
Language:English
Subjects:
Analytical, structural and metabolic biochemistry
ATPase
Biological and medical sciences
Cryoelectron microscopy
Energy coupling
Enzymes and enzyme inhibitors
Escherichia coli - enzymology
F1 F0
Freezing
Fundamental and applied biological sciences. Psychology
Hydrolases
Lipid Bilayers
Microscopy, Electron
Protein Conformation
Proton-Translocating ATPases - ultrastructure
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Summary:E. coli F1 F0 ATP synthase has been reconstituted into membranes and visualized by electron microscopy of unstained samples preserved in thin layers of amorphous ice. Unlike previous observations in negative stain, these specimens are not exposed to potentially denaturing or perturbing conditions, having been rapidly frozen from well‐defined conditions in which the enzyme is fully active. The structures visualized in views normal to the lipid bilayer clearly show the presence of a narrow stalk approx. 45 Å long, connecting the F1 to the membrane‐embedded F0.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(87)80234-X