Crystallization and preliminary crystallographic analysis of Abp, a GH27 β-L-arabinopyranosidase from Geobacillus stearothermophilus

A GH27 arabinopyranosidase from G. stearothermophilus (Abp) has been crystallized in the primitive orthorhombic space group P2₁2₁2₁. Full diffraction data sets have been measured for the wild-type enzyme and its D197A catalytic mutant to maximal resolutions of 2.28 and 2.30 Å, respectively, for use in a detailed three-dimensional structural analysis of the Abp protein.