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Topographical structure of membrane‐bound Escherichia coli F 1 F 0 ATP synthase in aqueous buffer
Author(s) -
Singh Seema,
Turina Paola,
Bustamante Carlos J.,
Keller David J.,
Capaldi Roderick
Publication year - 1996
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/s0014-5793(96)01127-1
Subject(s) - atp synthase , crystallography , protein subunit , chemistry , escherichia coli , dimple , aqueous solution , ring (chemistry) , molecular mass , microscopy , biology , biochemistry , enzyme , physics , optics , genetics , organic chemistry , gene
Scanning force microscope images of membrane‐bound Escherichia coli ATP synthase F 0 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 F 0 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 F 0 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.