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- W2047366765 abstract "We have investigated the structure of cytochrome c oxidase vesicle crystals by analysis at 20 Å resolution of electron micrographs of negatively stained specimens. The map clearly shows the shape of the part of the cytochrome c oxidase molecule which protrudes from the lipid bilayer. On the side of the membrane corresponding to the cytoplasmic face of the mitochondrial inner membrane, the molecule projects over 50 Å into solution. About half of the mass of the protein is in this domain, which contains the cytochrome c binding site. On the side of the membrane corresponding to the matrix face, no features are observed, which at this resolution means the protein protrudes less than 20 Å. In vesicle crystals, and probably in the mitochondrion, cytochrome c oxidase monomers are closely paired as dimers, with a clear cleft showing the boundary between monomers." @default.
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- W2047366765 date "1982-07-01" @default.
- W2047366765 modified "2023-09-23" @default.
- W2047366765 title "Three-dimensional structure of cytochrome c oxidase vesicle crystals in negative stain" @default.
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- W2047366765 doi "https://doi.org/10.1016/0022-2836(82)90210-8" @default.
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