Crystallization and preliminary crystallographic analysis of the glycoside hydrolase family 115 α-­glucuronidase from Streptomyces pristinaespiralis

摘要

α-Glucuronidase from Streptomyces pristinaespiralis (SpGlcA115A) is com­posed of a single-chain peptide containing a catalytic domain belonging to glycosyl hydrolase family 115, a novel family of hemicellulolytic α-glucuronidases. The enzyme catalyzes the hydrolysis of α-linked 4-O-methylglucuronosyl and glucuronosyl residues from both polymeric xylans and oligosaccharides. SpGlcA115A was crystallized at 293 K using the sitting-drop vapour-diffusion method. The crystals belonged to space group R3 and diffracted to a resolution of 1.9 Å.