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  • Title: Crystallization and preliminary crystallographic analysis of exo-alpha-1,5-L-arabinofuranosidase from Streptomyces avermitilis NBRC14893.
    Author: Fujimoto Z, Ichinose H, Kaneko S.
    Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun; 2008 Nov 01; 64(Pt 11):1007-9. PubMed ID: 18997327.
    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.
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