PMID:8941708

Citation	Singh, S, Turina, P, Bustamante, CJ, Keller, DJ and Capaldi, R (1996) Topographical structure of membrane-bound Escherichia coli F1F0 ATP synthase in aqueous buffer. FEBS Lett. 397:30-4
Abstract	Scanning force microscope images of membrane-bound Escherichia coli ATP synthase F0 complexes have been obtained in aqueous solution. The images show a consistent set of internal features: a ring structure which surrounds a central dimple and contains an asymmetric lateral mass. Images of trypsin-treated F0 complexes, which have lost part of their b subunits, show a reduced asymmetric mass, while images of c-subunit oligomers, which lack both the a and b subunits, show a ring and dimple but do not have an asymmetric mass. These results support models in which the F0 complex contains a ring of 9-12 c subunits with the b subunits located outside this ring, and show that scanning force microscopy is able to provide structural information on membrane proteins of molecular mass less than 200 000 Da.
Links	PubMed
Keywords	Escherichia coli/enzymology; Image Processing, Computer-Assisted; Membranes, Artificial; Microscopy; Phosphatidylethanolamines; Protein Conformation; Proton-Translocating ATPases/chemistry; Proton-Translocating ATPases/ultrastructure; Trypsin
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