Crystallization and preliminary X-ray study of alkaline β-mannanase from the alkaliphilic Bacillus sp. N16-5

The catalytic domain of an alkaline mannanase from the alkaliphilic Bacillus sp. N16-5 was expressed in E. coli and purified. Crystallization and preliminarily X-ray crystallographic analysis were performed for the recombinant enzyme. The catalytic domain of an alkaline β-mannanase from the alkaliphilic Bacillus sp. N16-5 has been expressed and purified. The recombinant enzyme was crystallized using the hanging-drop vapour-diffusion method at 298 K. X-ray diffraction data were collected to 1.6 Å resolution. The crystal belonged to the orthorhombic space group P2₁2₁2₁, with unit-cell parameters a = 59.03, b = 63.31, c = 83.34 Å. Initial phasing was carried out by molecular replacement using the three-dimensional structure of a mannanase from the alkaliphilic Bacillus sp. JAMB602 as a search model