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

Pernilla Turner, Anna Pramhed, Erik Kanders, Martin Hedström, Eva Nordberg Karlsson, Derek Logan

Forskningsoutput: TidskriftsbidragArtikel i vetenskaplig tidskriftPeer review

8 !!Citations (SciVal)

Sammanfattning

-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.
Originalspråkengelska
Sidor (från-till)802-806
TidskriftActa Crystallographica. Section F: Structural Biology and Crystallization Communications
Volym63
Utgåva9
DOI
StatusPublished - 2007

Ämnesklassifikation (UKÄ)

  • Biologiska vetenskaper
  • Industriell bioteknik

Fingeravtryck

Utforska forskningsämnen för ”Expression, purification, crystallisation and preliminary X-ray diffraction analysis of Thermotoga neapolitana beta-glucosidase B”. Tillsammans bildar de ett unikt fingeravtryck.

Citera det här