Crystallization and preliminary X-ray analysis of dimeric and trimeric cytochromes c from horse heart.
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 P2(1)2(1)2(1), 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.
Department of Life Science, Graduate School of Life Science, University of Hyogo, 3-2-1 Koto, Kamigori-cho, Ako-gun, Hyogo 678-1297, Japan.
Midori
M
Taketa
Hirofumi
H
Komori
Yoko
Y
Hattori
Satoshi
S
Nagao
Shun
S
Hirota
Yoshiki
Y
Higuchi
D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D045304:Cytochromes c / Q000737:chemistry*; D006736:Horses; D009206:Myocardium / Q000737:chemistry*; D055503:Protein Multimerization
D045304:Cytochromes c