Crystallization of the purine salvage enzyme adenine phosphoribosyltransferase.
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.
Phillíps
C L
CL
Department of Biochemistry and Molecular Biology, Oregon Health Sciences University, Portland 97201-3098, USA.
Ullman
B
B
Brennan
R G
RG
D000228:Adenine Phosphoribosyltransferase / Q000737:chemistry*; D000818:Animals; D003460:Crystallization; D007893:Leishmania donovani / Q000201:enzymology; D013237:Stereoisomerism; D014961:X-Ray Diffraction
D000228:Adenine Phosphoribosyltransferase