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.