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

The thioredoxin-related protein tryparedoxin I from Crithidia fasciculata has been crystallized using PEG 4000 as a precipitant. The enzyme forms long needle-shaped crystals which diffract to at least 1.7 Å. A native data set has been collected at the DESY synchrotron from a flash-frozen crystal at 90 K to 1.7 Å resolution. The data set shows that the crystals belong to the orthorhombic space group P2₁2₁2₁ and have unit-cell parameters a = 37.94, b = 51.39, c = 71.46 Å. Tryparedoxin I is involved in a trypanothione-dependent peroxide metabolic pathway specific for trypanosomatids 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.