Expression, purification, crystallization and preliminary x-ray diffraction analysis of uracil phosphoribosyltransferase of Toxoplasma gondii

Academic Article

Abstract

  • Recombinant uracil phosphoribosyltransferase (UPRT) enzyme of Toxoplasma gondii was expressed in Escherichia coli and purified from the cell-free extract by a combination of chromatographic steps. The recombinant protein was enzymatically active when tested in an in vitro UPRT assay. The purified protein was crystallized using the hanging-drop vapor-diffusion technique with ammonium phosphate as precipitant. The crystallized protein also exhibited UPRT activity. Crystals diffract to 2.4 Å resolution and belong to space group P3121 or P3221 with unit-cell dimensions a = b = 119.9, c = 70.8 Å and two molecules per asymmetric unit.
  • Digital Object Identifier (doi)

    Author List

  • Barchue J; Symersky J; Narayana SVL; Moore JK; DeLucas LJ; Chattopadhyay D
  • Start Page

  • 347
  • End Page

  • 349
  • Volume

  • 55
  • Issue

  • 1