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Abstract In the presence of phospholipid cardiolipin, the protein cytochrome c forms a water-insoluble complex that precipitates. The cardiolipin-to-cytochrome c molar ratio evaluated by centrifugation and spectrophotometry is ca. 35: 1. According to small-angle X-ray scattering data, the precipitate has a microcrystalline structure with interplanar spacings characterizing the crystal unit cell equal to 11.1 ± 1 nm. In the case of an insufficient amount of cardiolipin, the structure and spectroscopic properties of cytochrome c in the supernatant do not differ from those of an aqueous solution of cytochrome c.
Crystallography Reports – Springer Journals
Published: Jul 1, 2011
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