Crystallization and preliminary X-ray studies of V(1)-ATPase of Thermus thermophilus HB8 complexed with Mg-ADP.
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.
Ishii
N
N
Biophysical Chemistry Laboratory, National Institute of Bioscience and Human Technology, 1-1 Higashi, Tsukuba, Ibaraki, 305-8566, Japan. ishii@ni.aist.go.jp
Saijo
S
S
Sato
T
T
Tanaka
N
N
Harata
K
K
D000244:Adenosine Diphosphate / Q000494:pharmacology; D001426:Bacterial Proteins / Q000737:chemistry; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000295:instrumentation / Q000379:methods; D016963:Thermus thermophilus / Q000737:chemistry*; D025262:Vacuolar Proton-Translocating ATPases / Q000737:chemistry*
D001426:Bacterial Proteins; D000244:Adenosine Diphosphate; D025262:Vacuolar Proton-Translocating ATPases