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

Research output: Contribution to journalArticle


-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.


Research areas and keywords

Subject classification (UKÄ) – MANDATORY

  • Biological Sciences
  • Industrial Biotechnology


  • multiple-wavelength anomalous dispersion., selenomethionine incorporation, Thermotoga neapolitana, glycoside hydrolase family 3
Original languageEnglish
Pages (from-to)802-806
JournalActa Crystallographica. Section F: Structural Biology and Crystallization Communications
Issue number9
Publication statusPublished - 2007
Publication categoryResearch