Skip to main content
U.S. Department of Energy
Office of Scientific and Technical Information

Crystallization and preliminary X-ray diffraction studies of two thermostable α-galactosidases from glycoside hydrolase family 36

Journal Article · · Acta Crystallographica. Section F
 [1]; ;  [2];
  1. 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)
  2. Institut für Industrielle Genetik, Universität Stuttgart, Allmandring 31, D-70569 Stuttgart (Germany)

The α-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 Å resolution, respectively. α-Galactosidases from thermophilic organisms have gained interest owing to their applications in the sugar industry. The α-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 Å resolution, respectively. Crystals of AgaB belong to space group I222 or I2{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 87.5, b = 113.3, c = 161.6 Å. Crystals of AgaA A355E belong to space group P3{sub 1}21 or P3{sub 2}21, with unit-cell parameters a = b = 150.1, c = 233.2 Å.

OSTI ID:
22356274
Journal Information:
Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 2 Vol. 62; ISSN ACSFCL; ISSN 1744-3091
Country of Publication:
United Kingdom
Language:
English