4.0 Article

Xylanase B from Clostridium cellulovorans 743B: overexpression, purification, crystallization and X-ray diffraction analysis

Publisher

INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S2053230X18000341

Keywords

xylanases; xylanase B; Clostridium cellulovorans; cellulosome; CBM family 22; glycoside hydrolase family 10

Funding

  1. Programme for Promotion of Basic and Applied Research for Innovations in Bio-oriented Industry
  2. Science and Technology Research Promotion Program for Agriculture, Forestry, Fisheries, and Food Industry
  3. Japan Science and Technology Agency, Core Research for Evolutional Science and Technology

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Clostridium cellulovorans produces multi-enzyme complexes called cellulosomes capable of efficiently degrading cellulosic biomass. There are three xylanase genes containing a sequence corresponding to a dockerin domain that are necessary for constructing cellulosomes in the genome. Among the xylanases encoded by these genes, xylanase B (XynB) contains a catalytic domain belonging to glycoside hydrolase family 10 and a carbohydrate-binding module (CBM) at the N-terminus, making it a member of CBM family 22. In this study, XynB was cloned, overexpressed, purified and crystallized. XynB was crystallized using the hanging-drop vapour-diffusion method in the presence of 0.2 M sodium acetate trihydrate, 0.1 MTris-HCl pH 8.5, 32%(w/v) PEG 4000 at 293 K. X-ray diffraction analysis revealed that the crystal diffracted to 1.95 angstrom resolution and belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 74.28, b = 77.55, c = 88.20 angstrom, alpha = beta = gamma = 90 degrees. The data-evaluation statistics revealed high quality of the collected data, thereby establishing a solid basis for determination of the structure of cellulosomal xylanase from C. cellulovorans.

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