Crystallization and preliminary X-ray analysis of dimeric and trimeric cytochromes c from horse heart

Dimeric and trimeric cytochromes c were purified and crystallized. X-ray diffraction data sets were collected to resolutions of 2.2 and 2.1 Å, respectively. Cytochrome c (cyt c) is an electron-transfer protein in the respiratory chain of mitochondria. It is known to form polymers, but its polymerization mechanism is still unknown. Dimeric and trimeric cyt c from horse were successfully crystallized by the sitting-drop vapour-diffusion method using polyethylene glycol as a precipitating reagent. The crystal of dimeric cyt c belonged to space group P1, with unit-cell parameters a = 41.8, b = 56.3, c = 60.8 Å, α = 66.3, β = 89.9, γ = 73.7°, whereas that of trimeric cyt c belonged to space group P2₁2₁2₁, with unit-cell parameters a = 57.2, b = 95.7, c = 130.9 Å. Initial structure models showed that the crystals of dimeric and trimeric cyt c contained two dimers and two trimers, respectively, in the asymmetric unit