title: Crystallization of the purine salvage enzyme adenine phosphoribosyltransferase.
abstract: Adenine phosphoribosyltransferase from the protozoan parasite Leishmania donovani has been crystallized in the presence of the substrate Mg(2+)-alpha-D-5-phosphoribosyl-1-pyrophosphate (PRPP) or the product adenosine-5-monophosphate, as well as in the absence of ligand. These crystals belong to the space group P6(1)22 or its enantiomorph P6(5)22, with unit cell dimensions of a = b = 64.0 A, c = 240.5 A, alpha = beta = 90 degrees, and gamma = 120 degrees. The crystals diffract to 1.9 A.
authors.affiliation: Department of Biochemistry and Molecular Biology, Oregon Health Sciences University, Portland 97201-3098, USA.
authors.forename: C L
authors.initials: CL
authors.lastname: Phillíps
authors.forename: B
authors.initials: B
authors.lastname: Ullman
authors.forename: R G
authors.initials: RG
authors.lastname: Brennan
mesh_terms: D000228:Adenine Phosphoribosyltransferase / Q000737:chemistry*; D000818:Animals; D003460:Crystallization; D007893:Leishmania donovani / Q000201:enzymology; D013237:Stereoisomerism; D014961:X-Ray Diffraction
chemical_list: D000228:Adenine Phosphoribosyltransferase