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

被引：0
|
作者：
Foucault, M
Watzlawick, H
Mattes, R
Haser, R
Gouet, P
机构：
[1] UCBL, CNRS, UMR 5086, Inst Biol & Chim Prot,Lab Biocristallog,IFR 128,B, F-69367 Lyon 07, France
[2] Univ Stuttgart, Inst Ind Genet, D-70569 Stuttgart, Germany
来源：
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2006年 / 62卷
关键词：
D O I：
10.1107/S1744309105042582
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
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 over-expressed 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 angstrom 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 angstrom. 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 angstrom.
引用
收藏
页码：100 / 103
页数：4
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