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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.

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A rational double mutation in the serine acetyl xylo-oligosaccharide esterase from G. stearothermophilus T6 (Axe2) converts the enzyme from an octameric form to a dimeric form. The dimeric double mutant (Axe2-Y184F-W190P) has been crystallized in the orthorhombic space group P212121 and a complete X-ray diffraction data set has been measured for these crystals at 2.3 Å resolution for use in a full three-dimensional structural analysis of this form of the protein.

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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.
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