Nucleoside diphosphate kinase from the hyperthermophilic archaeon Methanococcus jannaschii: overexpression, crystallization and preliminary X-ray crystallographic analysis

Abstract

Nucleoside diphosphate (NDP) kinase is a key enzyme in maintaining cellular pools of all nucleoside triphosphates. NDP kinase from the hyperthermophilic archaebacterium Methanococcus jannaschii has been overexpressed in Escherichia coli and crystallized at 297 K using polyethylene glycol 4000 as precipitant. The crystal is hexagonal, belonging to the space group P6(3), with unit-cell parameters a = b = 72.89, c = 100.87 Angstrom. The asymmetric unit contains two subunits of NDP kinase, with a corresponding crystal volume 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 been collected using synchrotron X-rays.