Abstract
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-β-d-thioglucoside as detergent. The crystals diffract to 3.8 Å, belong to the space group P2 or P21 and have unit cell dimensions of a = 80.7 A ̊; b = 116.0 A ̊; c = 156.9 A ̊ and β = 104.4°. The asymmetric unit contains two ba3-type oxidase molecules.
Original language | English |
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Pages (from-to) | 132-134 |
Number of pages | 3 |
Journal | FEBS Letters |
Volume | 368 |
Issue number | 1 |
DOIs | |
Publication status | Published - 10 Jul 1995 |
Externally published | Yes |
Keywords
- ba-oxidase
- cytochrome-c oxidase
- Membrane protein crystallization
- Thermus thermophilus
- X-ray diffraction