Crystallization and preliminary X-ray analysis of the diadenosine 5',5'''-P1,P4-tetraphosphate phosphorylase from Mycobacterium tuberculosis H37Rv.
A novel diadenosine 5',5'''-P(1),P(4)-tetraphosphate (Ap4A) phosphorylase (Rv2613c) from Mycobacterium tuberculosis H37Rv has been crystallized by the sitting-drop vapour-diffusion method. The crystal belonged to space group C2, with unit-cell parameters a = 101.5, b = 63.6, c = 79.1 A, beta = 110.9 degrees. The diffraction of the crystals extended to 1.9 A resolution. The asymmetric unit is expected to contain two molecules of Rv2613c, with a corresponding crystal volume per protein weight (V(M)) of 2.41 A(3) Da(-1) and a solvent content of 49.1%. This is the first report of a crystal of Ap4A phosphorylase.
Mori
Shigetarou
S
Department of Bacteriology II, National Institute of Infectious Diseases, 4-7-1 Gakuen, Musashimurayama-shi, Tokyo 208-0011, Japan.
Shibayama
Keigo
K
Wachino
Jun-ichi
J
Arakawa
Yoshichika
Y
D003460:Crystallization; D018360:Crystallography, X-Ray; D009169:Mycobacterium tuberculosis / Q000201:enzymology*; D009713:Nucleotidyltransferases / Q000737:chemistry*
D009713:Nucleotidyltransferases; C044740:diadenosine 5,5'''-P(1),P(4)-tetraphosphate alpha,beta-phosphorylase