Crystallization and preliminary X-ray diffraction studies of two thermostable alpha-galactosidases from glycoside hydrolase family 36.
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| 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. |
| Year of Publication |
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2006
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| Journal |
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Acta crystallographica. Section F, Structural biology and crystallization communications
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| Volume |
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62
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| Issue |
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Pt 2
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| Number of Pages |
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100-3
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| Date Published |
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2006
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| URL |
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http://scripts.iucr.org/cgi-bin/paper?S1744309105042582
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| DOI |
:
10.1107/S1744309105042582
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| Short Title |
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Acta Crystallogr Sect F Struct Biol Cryst Commun
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