Open AccessCrystallization and preliminary X‐ray analysis of dimeric and trimeric cytochromes c from horse heart
Author(s) -
Taketa Midori,
Komori Hirofumi,
Hattori Yoko,
Nagao Satoshi,
Hirota Shun,
Higuchi Yoshiki
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110034913
Subject(s) - crystallization , crystallography , horse , x ray , chemistry , materials science , stereochemistry , physics , biology , organic chemistry , optics , paleontology
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 P 1, 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 P 2 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.