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- W1608237889 abstract "The crystal structure of oxidized cytochrome c from tuna hearts has been solved by x-ray diffraction to a resolution of 2.0 A, using four isomorphous heavy atom derivatives. The crystals, space group P43, have 2 independent cytochrome molecules in the asymmetric repeating unit. No significant difference is seen between these 2 molecules, aside from conformations of a few surface side chains. The molecular folding observed is essentially that reported for tuna ferrocytochrome c. In particular, the ring of phenylalanine 83 lies against the heme group and closes the heme crevice, and is not swung out into the surroundings as had been believed from the 2.8 A horse ferricytochrome c structure." @default.
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- W1608237889 date "1977-01-01" @default.
- W1608237889 modified "2023-10-06" @default.
- W1608237889 title "Tuna cytochrome c at 2.0 A resolution. I.Ferricytochrome structure analysis." @default.
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- W1608237889 doi "https://doi.org/10.1016/s0021-9258(17)32783-7" @default.
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