Purification, crystallization and preliminary crystallographic analysis of Gan1D, a GH1 6-phospho-β-galactosidase from Geobacillus stearothermophilus T1

A GH1 6-phospho-β-galactosidase from G. stearothermophilus T1 (Gan1D) has been purified and crystallized in the triclinic space group P1. A full diffraction data set has been measured for the wild-type enzyme to a maximal resolution of 1.33 Å to be further used for a detailed three-dimensional structural analysis of the protein.

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

A correction is made to the article by Lansky et al. [ (2013), Acta Cryst. F69, 430-434] .

Cloning, purification and preliminary crystallographic analysis of Ara127N, a GH127 β-L-arabinofuranosidase from Geobacillus stearothermophilus T6

A GH127 β-L-arabinofuranosidase from G. stearothermophilus T6 (Ara127N) has been purified and crystallized in two different crystal forms. A full X-ray diffraction data set was measured for the wild-type enzyme in a P2₁2₁2₁ crystal form (2.3 Å resolution) and complete MAD data were measured for the selenomethionine derivative in a P2₁ crystal form (2.5 Å resolution) to be used for the detailed three-dimensional structural analysis of the Ara127N protein.

Preliminary crystallographic analysis of Xyn52B2, a GH52 β-D-xylosidase from Geobacillus stearothermophilus T6

A GH52 β-D-xylosidase from G. stearothermophilus T6 (Xyn52B2) has been crystallized in a new orthorhombic P2₁2₁2₁ crystal form. Full X-ray diffraction data sets were measured for the wild-type enzyme (3.70 Å resolution), the E335G catalytic mutant (2.95 Å resolution), a potential Hg derivative (2.15 Å resolution) and a selenomethionine derivative (3.90 Å resolution) for use in a detailed three-dimensional structural analysis of the Xyn52B2 protein.