Purification, crystallization and preliminary X-ray analysis of a thermostable glycoside hydrolase family 43 β-xylosidase from Geobacillus thermoleovorans IT-08

Ali Rohman, Niels Van Oosterwijk, Slavko Kralj, Lubbert Dijkhuizen, Bauke W. Dijkstra, Ni Nyoman Tri Puspaningsih

Research output: Contribution to journalArticlepeer-review

6 Citations (Scopus)

Abstract

The main enzymes involved in xylan-backbone hydrolysis are endo-1,4-β-xylanase and β-xylosidase. β-Xylosidase converts the xylo-oligosaccharides produced by endo-1,4-β-xylanase into xylose monomers. The β-xylosidase from the thermophilic Geobacillus thermoleovorans IT-08, a member of glycoside hydrolase family 43, was crystallized at room temperature using the hanging-drop vapour-diffusion method. Two crystal forms were observed. Bipyramid-shaped crystals belonging to space group P432 12, with unit-cell parameters a = b = 62.53, c = 277.4 Å diffracted to 1.55 Å resolution. The rectangular crystals belonged to space group P21, with unit-cell parameters a = 57.94, b = 142.1, c = 153.9 Å, β = 90.5°, and diffracted to 1.80 Å resolution.

Original languageEnglish
Pages (from-to)932-935
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume63
Issue number11
DOIs
Publication statusPublished - 2007

Keywords

  • Geobacillus thermoleovorans IT-08
  • Glycoside hydrolase family 43
  • β-xylosidase

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