Crystallization and preliminary X-ray diffraction studies of two thermostable alpha-galactosidases from glycoside hydrolase family 36.
alpha-Galactosidases from thermophilic organisms have gained interest owing to their applications in the sugar industry. The alpha-galactosidases AgaA, AgaB and AgaA A355E mutant from Geobacillus stearothermophilus have been overexpressed in Escherichia coli. Crystals of AgaB and AgaA A355E have been obtained by the vapour-diffusion method and synchrotron data have been collected to 2.0 and 2.8 A resolution, respectively. Crystals of AgaB belong to space group I222 or I2(1)2(1)2(1), with unit-cell parameters a = 87.5, b = 113.3, c = 161.6 A. Crystals of AgaA A355E belong to space group P3(1)21 or P3(2)21, with unit-cell parameters a = b = 150.1, c = 233.2 A.
Foucault
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M
Institut de Biologie et Chimie des Protéines, CNRS-UCBL, UMR 5086, Laboratoire de Bio-Cristallographie IFR128 BioSciences Lyon-Gerland, 7 Passage du Vercors, 69367 Lyon Cedex 07, France.
Watzlawick
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H
Mattes
R
R
Haser
R
R
Gouet
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P
D001406:Bacillaceae / Q000201:enzymology / Q000235:genetics; D003460:Crystallization; D018360:Crystallography, X-Ray; D004795:Enzyme Stability / Q000235:genetics; D004926:Escherichia coli / Q000235:genetics; D017354:Point Mutation; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry; D013696:Temperature; D000519:alpha-Galactosidase / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics
D011994:Recombinant Proteins; D000519:alpha-Galactosidase