Crystallization and Preliminary X-Ray Crystallographic Studies of Trypanosoma brucei Prostaglandin F_2α Synthase

Abstract

Prostaglandin F_2α is a potent mediator of various physiological and pathological processes. Trypanosoma brucei prostaglandin F_2α synthase (TbPGFS) catalyzes the NADPH-dependent reduction of 9, 11-endoperoxide PGH₂ to PGF_2α, and could thus be involved in the elevation of the PGF_2α concentration during African trypanosomasis. In the present report, the purification and crystallization of recombinant TbPGFS are described. The active recombinant enzyme was crystallized by the hanging-drop vapor-diffusion method using ammonium sulfate as a precipitant. The crystal belonged to a tetragonal space group, P4₁2₁2 or P4₃2₁2, with unit-cell parameters of a=b=112.3 Å, and c=140.0 Å. Native data up to 2.6 Å resolution were collected from the crystal using our home facility.