Three-dimensional crystals of cytochrome-c oxidase from Thermus thermophilus diffracting to 3.8 A resolution.
The ba3-type cytochrome-c oxidase from Thermus thermophilus has been crystallized in its native form. Crystallization was achieved by the batch and the vapour diffusion sitting drop methods using polyethylene glycol monomethyl ether 2000 as precipitating agent in the presence of octyl-beta-D-thioglucoside as detergent. The crystals diffract to 3.8 A, belong to the space group P2 or P2(1) and have unit cell dimensions of a = 80.7 A; b = 116.0 A; c = 156.9 A and beta = 104.4 degrees. The asymmetric unit contains two ba3-type oxidase molecules.
Soulimane
T
T
Rheinisch-Westfälische Technische Hochschule, Institut für Biochemie, Klinikum Aachen, Germany.
Gohlke
U
U
Huber
R
R
Buse
G
G
D018360:Crystallography, X-Ray; D003576:Electron Transport Complex IV / Q000737:chemistry*; D011487:Protein Conformation; D016963:Thermus thermophilus / Q000201:enzymology*
D003576:Electron Transport Complex IV