Three-dimensional crystals of cytochrome-c oxidase from Thermus thermophilus diffracting to 3.8 Å resolution

Tewfik Soulimane, Ulrich Gohlke, Robert Huber, Gerhard Buse

Research output: Contribution to journalArticlepeer-review

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 languageEnglish
Pages (from-to)132-134
Number of pages3
JournalFEBS Letters
Volume368
Issue number1
DOIs
Publication statusPublished - 10 Jul 1995
Externally publishedYes

Keywords

  • ba-oxidase
  • cytochrome-c oxidase
  • Membrane protein crystallization
  • Thermus thermophilus
  • X-ray diffraction

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