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Crystallization and preliminary X-ray studies of V(1)-ATPase of Thermus thermophilus HB8 complexed with Mg-ADP.
Ishii, N; Saijo, S; Sato, T; Tanaka, N; Harata, K.
Affiliation
  • Ishii N; Biophysical Chemistry Laboratory, National Institute of Bioscience and Human Technology, 1-1 Higashi, Tsukuba, Ibaraki, 305-8566, Japan. ishii@ni.aist.go.jp
J Struct Biol ; 134(1): 88-92, 2001 Apr.
Article in En | MEDLINE | ID: mdl-11469881
ABSTRACT
Crystals have been grown of the V(1)-ATPase sector of the V-type ATP synthase complex (V(0)V(1)) from the thermophilic eubacterium Thermus thermophilus HB8. These crystals are grown by the vapor diffusion method in the presence of 5 mM Mg-ADP, from solutions containing 100 mM sodium acetate and 2 M sodium formate, pH 5.5. The crystals diffracted X rays beyond 3.4 A in resolution on a synchrotron radiation source. The crystals belong to the trigonal space group P3, with unit cell dimensions of a = b = 89.0 A, c = 179.2 A, and gamma = 120 degrees. The unit cell presumably contains one molecule of V(1)-ATPase and the V(m) value is calculated as 3.0 A(3)/Da.
Subject(s)
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Collection: 01-internacional Database: MEDLINE Main subject: Thermus thermophilus / Vacuolar Proton-Translocating ATPases Language: En Journal: J Struct Biol Journal subject: BIOLOGIA MOLECULAR Year: 2001 Document type: Article Affiliation country: Japan
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Collection: 01-internacional Database: MEDLINE Main subject: Thermus thermophilus / Vacuolar Proton-Translocating ATPases Language: En Journal: J Struct Biol Journal subject: BIOLOGIA MOLECULAR Year: 2001 Document type: Article Affiliation country: Japan