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The stalk connecting the F 1 and F 0 domains of ATP synthase visualized by electron microscopy of unstained specimens
Author(s) -
Gogol Edward P.,
Lücken Uwe,
Capaldi Roderick A.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80234-x
Subject(s) - atp synthase , electron microscope , negative stain , lipid bilayer , microscopy , crystallography , chemistry , membrane , stalk , bilayer , biophysics , analytical chemistry (journal) , enzyme , biology , biochemistry , optics , physics , chromatography , horticulture
E. coli F 1 F 0 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 F 1 to the membrane‐embedded F 0 .