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Expression, purification, crystallisation and preliminary X-ray diffraction analysis of Thermotoga neapolitana beta-glucosidase B

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Author

Summary, in English

-Glucosidases belong to families 1, 3 and 9 of the glycoside hydrolases and act on cello-oligosaccharides. Family 1 and 3 enzymes are retaining and are reported to have transglycosylation activity, which can be used to produce oligosaccharides and glycoconjugates. Family 3 enzymes are less well characterized than their family 1 homologues and to date only two crystal structures have been solved. Here, the expression, purification, crystallization and X-ray diffraction data of a family 3 -glucosidase from the hyperthermophilic bacterium Thermotoga neapolitana are reported. Crystals of selenomethionine-substituted protein have also been grown. The crystals belong to space group C2221, with unit-cell parameters a = 74.9, b = 127.0, c = 175.2 Å. Native data have been collected to 2.4 Å resolution and the structure has been solved to 2.7 Å using the selenomethionine MAD method. Model building and refinement of the structure are under way.

Publishing year

2007

Language

English

Pages

802-806

Publication/Series

Acta Crystallographica. Section F: Structural Biology and Crystallization Communications

Volume

63

Issue

9

Document type

Journal article

Publisher

Wiley-Blackwell

Topic

  • Biological Sciences
  • Industrial Biotechnology

Keywords

  • multiple-wavelength anomalous dispersion.
  • selenomethionine incorporation
  • Thermotoga neapolitana
  • glycoside hydrolase family 3

Status

Published

ISBN/ISSN/Other

  • ISSN: 2053-230X