Electron microscopy of two-dimensional crystals of mitochondrial ATP synthase.
Two-dimensional crystals of the mitochondrial ATP synthase up to 0.4 microns in size were obtained from the detergent-lipid-protein micelles by detergent dialysis. A projected map of the negatively stained crystal was calculated from electron microscopical images by the Fourier-filtering procedure at about 2.8 nm resolution. The unit cell (with not more than two ATP synthase molecules) has the following parameters: a = 13.0 nm, b = 25.6 nm and gamma = 86 degrees. Two alternative models for the crystal structural organization were suggested, viz. with one or two protein molecules per unit cell.
Dubachev
G E
GE
M.M. Shemyakin and Yu.A. Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow.
Lunev
A V
AV
Barnakov
A N
AN
Belogrudov
G I
GI
Grinkevich
V A
VA
Demin
V V
VV
D000818:Animals; D002417:Cattle; D003460:Crystallization; D005583:Fourier Analysis; D008854:Microscopy, Electron; D008929:Mitochondria, Heart / Q000201:enzymology*; D006180:Proton-Translocating ATPases / Q000737:chemistry / Q000648:ultrastructure
D006180:Proton-Translocating ATPases