Crystallization of RecombinantCrithidia fasciculataTryparedoxin

Recombinant tryparedoxin, a thioredoxin homologue fromCrithidia fasciculata,has been purified from anEscherichia coliexpression system and used in crystallization trials. Orthorhombic needles in space groupP212121, with unit cell dimensions ofa= 38.63,b= 51.47, andc= 73.41 Å, have been obtained. The crystals present a monomer of approximate molecular mass 16 kDa in the asymmetric unit and diffract to 1.8-Å resolution using synchrotron radiation. Structure determination will be carried out to further the understanding of the role tryparedoxin plays in regulating oxidative stress in parasitic trypanosomatids.