Crystallization and preliminary X‐ray analysis of Thermoactinomyces vulgaris R‐47 maltooligosaccharide‐metabolizing enzyme homologous to glucoamylase
A maltooligosaccharide‐metabolizing enzyme from Thermoactinomyces vulgaris R‐47 (TGA) homologous to glucoamylase degrades maltooligosaccharides more efficiently than starch, unlike fungal glucoamylases. TGA was crystallized and the state of the protein in solution was analyzed by gel‐filtration chromatography. Diffraction data were collected to 3.31 Å resolution. The TGA crystal belongs to the orthorhombic space group P212121 or P21212, with unit‐cell parameters a = 110.2, b = 317.6, c = 144.9 Å, and is expected to contain five to eight TGA molecules per asymmetric unit. Gel‐filtration and native PAGE analyses indicated that TGA exists as a dimer in solution. This is the first report of the crystallization of an oligomeric glucoamylase.
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Keywords: maltooligosaccharide‐metabolizing enzyme
Document Type: Research Article
Publication date: March 1, 2005