title: Crystallization and preliminary X-ray diffraction studies of two thermostable alpha-galactosidases from glycoside hydrolase family 36.
abstract: 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.
authors.affiliation: 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.
authors.forename: M
authors.initials: M
authors.lastname: Foucault
authors.forename: H
authors.initials: H
authors.lastname: Watzlawick
authors.forename: R
authors.initials: R
authors.lastname: Mattes
authors.forename: R
authors.initials: R
authors.lastname: Haser
authors.forename: P
authors.initials: P
authors.lastname: Gouet
mesh_terms: 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
chemical_list: D011994:Recombinant Proteins; D000519:alpha-Galactosidase