Crystallization and preliminary crystallographic analysis of Axe2, an acetylxylan esterase from Geobacillus stearothermophilus

The serine acetylxylan esterase from G. stearothermophilus (Axe2) has been crystallized in the tetragonal space group I422. Complete diffraction data sets have been measured for the selenomethionine derivative (SAD data, 1.70 Å resolution) and the wild-type enzyme (1.85 Å resolution) to be used for a full three-dimensional structural analysis of the Axe2 protein.

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.

Crystallization and preliminary crystallographic analysis of GanB, a GH42 intracellular β-galactosidase from Geobacillus stearothermophilus

The GH42 β-galactosidase GanB from G. stearothermophilus has been crystallized in the primitive orthorhombic space group P2₁2₁2₁. Complete diffraction data sets have been measured for the wild-type enzyme (2.45 Å resolution) and its catalytic mutant (E323A; 2.50 Å resolution) for use in a full three-dimensional structural analysis of the GanB protein.