title: Crystallization and preliminary X-ray crystallographic studies of XynX, a family 10 xylanase from Aeromonas punctata ME-1.
abstract: Xylanases catalyze the hydrolysis of beta-1,4-glycosidic linkages within the xylan backbone. XynX is a xylanase from Aeromonas punctata ME-1 and belongs to glycoside hydrolase family 10. While most xylanases show endo-type catalytic activities, XynX shows exo-like catalytic activities, selectively producing xylobiose from birchwood xylan. In this study, XynX was crystallized by the hanging-drop vapour-diffusion method. The crystals belonged to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 79.0, b = 88.6, c = 93.2 A, and diffracted to beyond 1.8 A resolution.
authors.affiliation: Department of Biochemistry, National Institute of Agrobiological Sciences, Tsukuba 305-8602, Japan. zui@affrc.go.jp
authors.forename: Zui
authors.initials: Z
authors.lastname: Fujimoto
authors.forename: Kengo
authors.initials: K
authors.lastname: Usui
authors.forename: Yukari
authors.initials: Y
authors.lastname: Kondo
authors.forename: Kazumasa
authors.initials: K
authors.lastname: Yasui
authors.forename: Keiichi
authors.initials: K
authors.lastname: Kawai
authors.forename: Tohru
authors.initials: T
authors.lastname: Suzuki
mesh_terms: D000333:Aeromonas / Q000201:enzymology*; D001426:Bacterial Proteins / Q000737:chemistry / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray; D043364:Endo-1,4-beta Xylanases / Q000737:chemistry* / Q000302:isolation & purification
chemical_list: D001426:Bacterial Proteins; D043364:Endo-1,4-beta Xylanases