Electron density profile of two-dimensionally crystalline membranous cytochrome c oxidase at low resolution.
Unilamellar vesicles of membranous cytochrome c oxidase have been isolated whose distribution of protein in the membrane plane was predominantly crystalline. The vesicles were collapsed via controlled partial dehydration, resulting, at first, in the formation of unoriented, mostly unstacked, membrane pairs. Further controlled partial dehydration resulted in the formation of oriented multilayers of stacks of membrane pairs, retaining the in-plane crystallinity. The above were monitored by electron microscopy and x-ray diffraction. Analysis of the x-ray diffraction from unoriented, unstacked membrane pairs by two independent methods provided the membrane electron density profile to 30 A resolution.
D000818:Animals; D002417:Cattle; D003460:Crystallization; D003576:Electron Transport Complex IV / Q000378:metabolism*; D007425:Intracellular Membranes / Q000201:enzymology; D008081:Liposomes; D008565:Membrane Proteins / Q000378:metabolism*; D008854:Microscopy, Electron; D008929:Mitochondria, Heart / Q000201:enzymology; D014961:X-Ray Diffraction
D008081:Liposomes; D008565:Membrane Proteins; D003576:Electron Transport Complex IV