CRYSTALLIZATION OF THE PURINE SALVAGE ENZYME ADENINE PHOSPHORIBOSYLTRANSFERASE

Adenine phosphoribosyltransferase from the protozoan parasite Leishman ia donovani has been crystallized in the presence of the substrate Mg2 +-alpha-D-5-phosphoribosyl-1-pyrophosphate (PRPP) or the product adeno sine-5-monophosphate, as well as in the absence of ligand. These cryst als belong to the space group P6(1)22 or its enantiomorph P6(5)22, wit h unit cell dimensions of a = b = 64.0 Angstrom, c = 240.5 Angstrom, a lpha = beta = 90 degrees, and gamma = 120 degrees. The crystals diffra ct to 1.9 Angstrom. (C) 1996 Wiley-Liss, Inc.