Preparation and crystallization of selenomethionyl dextranase from Penicillium minioluteum expressed in Pichia pastoris

Acta Crystallogr D Biol Crystallogr. 2002 Feb;58(Pt 2):346-8. doi: 10.1107/s0907444901020406. Epub 2002 Jan 24.

Abstract

Dextranase from the fungus Penicillium minioluteum hydrolyses alpha-1,6-glycosidic bonds in dextran polymers. The enzyme has been expressed in Pichia pastoris in the presence of selenomethionine (SeMet). The level of SeMet incorporation was estimated by amino-acid analysis to be 50%. The protein has been crystallized in space group P2(1)2(1)2, with unit-cell parameters a = 103.6, b = 115.3, c = 49.8 A and one molecule per asymmetric unit. The crystals diffract to 2.0 A and the presence of SeMet in the crystals has been confirmed by an X-ray absorption spectrum.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallization
  • Crystallography, X-Ray
  • Dextranase / chemistry*
  • Dextranase / genetics
  • Dextranase / isolation & purification
  • Penicillium / enzymology*
  • Pichia / genetics
  • Protein Conformation
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Selenomethionine / chemistry*

Substances

  • Recombinant Proteins
  • Selenomethionine
  • Dextranase