ArticleActa crystallographica. Section F, Structural biology and crystallization communications2009
Crystallization and preliminary crystallographic analysis of beta-L-arabinopyranosidase from Streptomyces avermitilis NBRC14893.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- A comparison of gas stream cooling and plunge cooling of macromolecular crystals.Journal of applied crystallography · 2019Article
- Arabinogalactan proteins: focus on carbohydrate active enzymes.Frontiers in plant science · 2014Review
- Characterization of an endo-processive-type xyloglucanase having a β-1,4-glucan-binding module and an endo-type xyloglucanase from Streptomyces avermitilis.Applied and environmental microbiology · 2012Article
- Crystallization of selenomethionyl exo-beta-1,3-galactanase from the basidiomycete Phanerochaete chrysosporium.Acta crystallographica. Section F, Structural biology and crystallization communications · 2009Article
- A beta-l-Arabinopyranosidase from Streptomyces avermitilis is a novel member of glycoside hydrolase family 27.The Journal of biological chemistry · 2009Article
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Authors and funding
6 authors.
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Abstract
Beta-L-arabinopyranosidase from Streptomyces avermitilis NBRC14893 is a monomeric protein consisting of a catalytic domain belonging to glycosyl hydrolase family 27, an unknown domain and a substrate-binding domain belonging to carbohydrate-binding module family 13. The complete enzyme (residues 45-658) has successfully been cloned and homologously expressed in the Streptomyces expression system. beta-L-Arabinopyranosidase was crystallized by the sitting-drop vapour-diffusion method. The crystals diffracted to 1.6 A resolution and belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 68.2, b = 98.9, c = 181.3 A. The Matthews coefficient was calculated to be 2.38 A(3) Da(-1).
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