Crystallization and preliminary X-ray crystallographic studies of XynX, a family 10 xylanase from Aeromonas punctata ME-1.
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.
Fujimoto
Zui
Z
Department of Biochemistry, National Institute of Agrobiological Sciences, Tsukuba 305-8602, Japan. zui@affrc.go.jp
Usui
Kengo
K
Kondo
Yukari
Y
Yasui
Kazumasa
K
Kawai
Keiichi
K
Suzuki
Tohru
T
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
D001426:Bacterial Proteins; D043364:Endo-1,4-beta Xylanases