title: Crystallization and preliminary crystallographic analysis of exo-alpha-1,5-L-arabinofuranosidase from Streptomyces avermitilis NBRC14893.
abstract: Exo-alpha-1,5-L-arabinofuranosidase from Streptomyces avermitilis NBRC14893 (SaAraf43A) is composed of a single-chain peptide containing a catalytic domain belonging to glycosyl hydrolase family 43 and a substrate-binding domain belonging to carbohydrate-binding module family 42. The enzyme catalyzes the hydrolysis of an alpha-linked L-arabinofuranosyl residue from hemicelluloses. SaAraf43A was crystallized at 293 K using the sitting-drop vapour-diffusion method. The crystals belonged to space group P2(1)2(1)2(1) and diffracted to a resolution of 2.2 A.
authors.affiliation: Protein Research Unit, National Institute of Agrobiological Sciences, 2-1-2 Kannondai, Tsukuba, Ibaraki 305-8602, Japan.
authors.forename: Zui
authors.initials: Z
authors.lastname: Fujimoto
authors.forename: Hitomi
authors.initials: H
authors.lastname: Ichinose
authors.forename: Satoshi
authors.initials: S
authors.lastname: Kaneko
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry*; D003460:Crystallization / Q000379:methods*; D018360:Crystallography, X-Ray; D006026:Glycoside Hydrolases / Q000737:chemistry*; D008969:Molecular Sequence Data; D013302:Streptomyces / Q000201:enzymology*; D017356:Synchrotrons; D014961:X-Ray Diffraction
chemical_list: D001426:Bacterial Proteins; D006026:Glycoside Hydrolases