Crystallization and preliminary X-ray analysis of a family 51 glycoside hydrolase, the alpha-l-arabinofuranosidase from Geobacillus stearothermophilus T-6.
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Hovel K, Shallom D, Niefind K, Baasov T, Shoham G, Shoham Y, Schomburg D
Crystallization and preliminary X-ray analysis of a family 51 glycoside hydrolase, the alpha-l-arabinofuranosidase from Geobacillus stearothermophilus T-6.
Acta Crystallogr D Biol Crystallogr. 2003 May;59(Pt 5):913-5. Epub 2003 Apr 25.
- PubMed ID
- 12777810 [ View in PubMed]
- Abstract
Alpha-l-arabinofuranosidases (EC 3.2.1.55) are hemicellulases that cleave the glycosidic bond between l-arabinofuranoside side chains and various oligosaccharides. In this study, the first crystallization and preliminary X-ray analysis of the alpha-l-arabinofuranosidase from Geobacillus stearothermophilus T-6 (AbfA T-6), a family 51 glycoside hydrolase, is described. AbfA T-6 is a hexameric protein consisting of six identical subunits of 502 amino acids and with a calculated molecular mass of 57 218 Da. Purified recombinant native and selenomethionine-containing AbfA T-6 were crystallized by the sitting-drop method in two different space groups, P2(1) (unit-cell parameters a = 100.8, b = 178.1, c = 196.2 A, beta = 96.1 degrees ) and R3 (unit-cell parameters a = b = 179.3, c = 100.4 A). The R3 crystals diffracted X-rays to a resolution of 1.8 A.