Alphey M S, Tetaud E, Gourley D G, Fairlamb A H, Hunter W N
Department of Biochemistry, University of Dundee, Dundee, DD1 5EH, United Kingdom.
J Struct Biol. 1999 Jun 1;126(1):76-9. doi: 10.1006/jsbi.1999.4091.
Recombinant tryparedoxin, a thioredoxin homologue from Crithidia fasciculata, has been purified from an Escherichia coli expression system and used in crystallization trials. Orthorhombic needles in space group P212121, with unit cell dimensions of a = 38.63, b = 51. 47, and c = 73.41 A, have been obtained. The crystals present a monomer of approximate molecular mass 16 kDa in the asymmetric unit and diffract to 1.8-A 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.
