Crystallization and preliminary X-ray analysis of NAD kinase from Mycobacterium tuberculosis H37Rv.
NAD kinase from Mycobacterium tuberculosis H37Rv utilizes ATP or inorganic polyphosphate [poly(P)] as a phosphoryl donor for the phosphorylation of NAD. The enzyme overexpressed in Escherichia coli was purified and crystallized by means of the hanging-drop vapour-diffusion method with polyethylene glycol 4000 as the precipitant. Preliminary X-ray analysis of the resultant crystals revealed they belonged to the monoclinic space group C2 and had unit-cell parameters a = 140.0, b = 69.3, c = 106.3 A, beta = 130.1 degrees. The molecular weight of the NAD kinase is 35 kDa; assuming that a crystal contains two subunits of the NAD kinase in an asymmetric unit, the solvent content V(sol) is 0.62. X-ray diffraction data to 2.99 A have been collected from the native crystal.
Mori
S
S
Department of Basic and Applied Molecular Biotechnology, Graduate School of Kyoto University, Uji, Kyoto 611-0011, Japan.
Kawai
S
S
Mikami
B
B
Murata
K
K
D003460:Crystallization; D018360:Crystallography, X-Ray; D009169:Mycobacterium tuberculosis / Q000201:enzymology*; D017853:Phosphotransferases (Alcohol Group Acceptor) / Q000737:chemistry*; D011487:Protein Conformation
D017853:Phosphotransferases (Alcohol Group Acceptor); C021844:NAD kinase