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Crystallization of the purine salvage enzyme adenine phosphoribosyltransferase (1996)

Phillips, Cynthia L. ; Ullman, Buddy ; Brennan, Richard G.

New York, NY : Wiley-Blackwell

Proteins: Structure, Function, and Genetics 25 (1996), S. 510-513

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ISSN: 0887-3585

Keywords: Leishmania ; parasite metabolism ; selenomethionine ; x-ray diffraction ; Chemistry ; Biochemistry and Biotechnology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Medicine

Notes: Adenine phosphoribosyltransferase from the protozoan parasite Leishmania donovani has been crystallized in the presence of the substrate Mg2+-α-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 P6122 or its enantiomorph P6522, with unit cell dimensions of a = b = 64.0 Å, c = 240.5 Å, α = β = 90°, and γ = 120°. The crystals diffract to 1.9 Å. © 1996 Wiley-Liss, Inc.

Additional Material: 1 Tab.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1002/prot.11

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