title: Crystallization and preliminary X-ray crystallographic study of Streptomyces olivaceoviridis E-86 beta-xylanase.
abstract: beta-Xylanase from Streptomyces olivaceoviridis E-86 has been crystallized by the hanging drop vapor diffusion method from 25% saturated ammonium sulfate and 2% McIlvaine buffer, pH 5.7. The crystals diffract to at least 1.9 A resolution, and belong to space group P2(1)2(1)2(1), with unit-cell dimensions of a=79.6 A, b=95.2 A, and c=140.3 A. There are probably two xylanase molecules (MW=45 K) per asymmetric unit.
authors.affiliation: Department of Biotechnology, National Institute of Agrobiological Resources, Tsukuba, Ibaraki.
authors.forename: Z
authors.initials: Z
authors.lastname: Fujimoto
authors.forename: H
authors.initials: H
authors.lastname: Mizuno
authors.forename: A
authors.initials: A
authors.lastname: Kuno
authors.forename: S
authors.initials: S
authors.lastname: Yoshida
authors.forename: H
authors.initials: H
authors.lastname: Kobayashi
authors.forename: I
authors.initials: I
authors.lastname: Kusakabe
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D015394:Molecular Structure; D013302:Streptomyces / Q000201:enzymology*; D043325:Xylan Endo-1,3-beta-Xylosidase; D014995:Xylosidases / Q000737:chemistry*
chemical_list: D014995:Xylosidases; D043325:Xylan Endo-1,3-beta-Xylosidase