Crystallization of recombinant Crithidia fasciculata tryparedoxin

Recombinant tryparedoxin, a thioredoxin homologue from Crithidia fasciculat a, has been purified from an Escherichia coli expression system and used in crystallization trials. Orthorhombic needles in space group P2(1)2(1)2(1) with unit cell dimensions of a = 38.63, b = 51.47, and c = 73.41 Angstrom, have been obtained. The crystals present a monomer of approximate molecular mass 16 kDa in the asymmetric unit and diffract to 1.8-Angstrom resolution using synchrotron radiation. Structure determination will be carried out t o further the understanding of the; role tryparedoxin plays in regulating o xidative stress in parasitic trypanosomatids. (C) 1999 Academic Press.