K. Min et al., Nucleoside diphosphate kinase from the hyperthermophilic archaeon Methanococcus jannaschii: overexpression, crystallization and preliminary X-ray crystallographic analysis, ACT CRYST D, 56, 2000, pp. 1485-1487
Nucleoside diphosphate (NDP) kinase is a key enzyme in maintaining cellular
pools of all nucleoside triphosphates. NDP kinase from the hyperthermophil
ic archaebacterium Methanococcus jannaschii has been overexpressed in Esche
richia coli and crystallized at 297 K using polyethylene glycol 4000 as pre
cipitant. The crystal is hexagonal, belonging to the space group P6(3), wit
h unit-cell parameters a = b = 72.89, c = 100.87 Angstrom. The asymmetric u
nit contains two subunits of NDP kinase, with a corresponding crystal volum
e per protein mass (V-M) of 2.38 Angstrom (3) Da(-1) and a solvent content
of 48.3%. Native X-ray diffraction data to 2.30 Angstrom resolution have be
en collected using synchrotron X-rays.