Literature DB >> 7615066

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

T Soulimane1, U Gohlke, R Huber, G Buse.   

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-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.

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Year:  1995        PMID: 7615066     DOI: 10.1016/0014-5793(95)00623-h

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  4 in total

1.  Primary structure of a novel subunit in ba3-cytochrome oxidase from Thermus thermophilus.

Authors:  T Soulimane; M E Than; M Dewor; R Huber; G Buse
Journal:  Protein Sci       Date:  2000-11       Impact factor: 6.725

2.  Structure and mechanism of the aberrant ba(3)-cytochrome c oxidase from thermus thermophilus.

Authors:  T Soulimane; G Buse; G P Bourenkov; H D Bartunik; R Huber; M E Than
Journal:  EMBO J       Date:  2000-04-17       Impact factor: 11.598

3.  Interaction of octyl-beta-thioglucopyranoside with lipid membranes.

Authors:  M R Wenk; J Seelig
Journal:  Biophys J       Date:  1997-11       Impact factor: 4.033

4.  Evidence for a copper-coordinated histidine-tyrosine cross-link in the active site of cytochrome oxidase.

Authors:  G Buse; T Soulimane; M Dewor; H E Meyer; M Blüggel
Journal:  Protein Sci       Date:  1999-05       Impact factor: 6.725

  4 in total

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