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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 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.
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