ArticleActa crystallographica. Section F, Structural biology and crystallization communications2008
Crystallization and preliminary crystallographic analysis of exo-alpha-1,5-L-arabinofuranosidase from Streptomyces avermitilis NBRC14893.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
- Crystal structure and characterization of the glycoside hydrolase family 62 α-L-arabinofuranosidase from Streptomyces coelicolor.The Journal of biological chemistry · 2014Article
- Crystal structure of an Exo-1,5-{alpha}-L-arabinofuranosidase from Streptomyces avermitilis provides insights into the mechanism of substrate discrimination between exo- and endo-type enzymes in glycoside hydrolase family 43.The Journal of biological chemistry · 2010Article
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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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