These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Crystallization and preliminary X-ray diffraction analysis of a novel GH120 β-xylosidase (XylC) from Thermoanaerobacterium saccharolyticum JW/SL-YS485.
    Author: Liu W, Sun Y, Ko TP, Wiegel J, Shao W, Lu F, Guo RT, Huang CH.
    Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun; 2012 Aug 01; 68(Pt 8):914-6. PubMed ID: 22869121.
    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.
    [Abstract] [Full Text] [Related] [New Search]