Crystallization and preliminary X-ray analysis of tryparedoxin I from Crithidia fasciculata

The thioredoxin-related protein tryparedoxin I from Crithidia fasciculata h as been crystallized using PEG 4000 as a precipitant. The enzyme forms long needle-shaped crystals which diffract to at least 1.7 Angstrom. A native d ata set has been collected at the DESY synchrotron from a hash-frozen cryst al at 90 K to 1.7 K resolution. The data set shows that the crystals belong to the orthorhombic space group P2(1)2(1)2(1) and have unit-cell parameter s a = 37.94, b = 51.39, c = 71.36 Angstrom. Tryparedoxin I is involved in a trypanothione-dependent peroxide metabolic pathway specific for trypanosom atids and may therefore be a suitable candidate for the design of drugs for the specific treatment of a variety of important tropical diseases caused by these parasites.