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Three‐dimensional crystals of cytochrome‐ c oxidase from Thermus thermophilus diffracting to 3.8 Å resolution
Author(s) -
Soulimane Tewfik,
Gohlke Ulrich,
Huber Robert,
Buse Gerhard
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00623-h
Subject(s) - thermus thermophilus , crystallization , polyethylene glycol , cytochrome c oxidase , crystallography , chemistry , cytochrome , stereochemistry , organic chemistry , biochemistry , enzyme , escherichia coli , gene
The ba 3 ‐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‐β‐ d ‐thioglucoside as detergent. The crystals diffract to 3.8 Å, belong to the space group P2 or P2 1 and have unit cell dimensions of ; ; and β = 104.4°. The asymmetric unit contains two ba 3 ‐type oxidase molecules.