title: Crystallization and preliminary X-ray diffraction analysis of a novel GH120 β-xylosidase (XylC) from Thermoanaerobacterium saccharolyticum JW/SL-YS485.
abstract: Xylosidases hydrolyze xylopolymers at the nonreducing end to free xylose units. The β-xylosidase (XylC) from Thermoanaerobacterium saccharolyticum JW/SL-YS485 was expressed in Escherichia coli and the recombinant protein was purified and crystallized. A BLASTP search with the XylC protein sequence showed that no similar structure had previously been solved. XylC was classified as a member of the new glycoside hydrolase family GH120 according to the CAZy website (http://www.cazy.org/). Crystals belonging to the monoclinic space group P2(1), with unit-cell parameters a = 88.36, b = 202.20, c = 99.87 Å, β = 99.04°, were obtained by the sitting-drop vapour-diffusion method and diffracted to 2.2 Å resolution. Structure determination using MIR and MAD methods is in progress.
authors.affiliation: Tianjin Key Laboratory of Industrial Microbiology, College of Biotechnology, Tianjin University of Science and Technology, Tianjin 300457, People's Republic of China.
authors.forename: Wenting
authors.initials: W
authors.lastname: Liu
authors.forename: Yu
authors.initials: Y
authors.lastname: Sun
authors.forename: Tzu-Ping
authors.initials: TP
authors.lastname: Ko
authors.forename: Juergen
authors.initials: J
authors.lastname: Wiegel
authors.forename: Weilan
authors.initials: W
authors.lastname: Shao
authors.forename: Fuping
authors.initials: F
authors.lastname: Lu
authors.forename: Rey-Ting
authors.initials: RT
authors.lastname: Guo
authors.forename: Chun-Hsiang
authors.initials: CH
authors.lastname: Huang
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D046950:Thermoanaerobacterium / Q000201:enzymology*; D014995:Xylosidases / Q000737:chemistry*
chemical_list: D014995:Xylosidases; C026579:exo-1,4-beta-D-xylosidase