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...

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Veröffentlicht in:	Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 1996-08, Vol.25 (4), p.510-513
Hauptverfasser:	Phillíps, C L, Ullman, B, Brennan, R G
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenine Phosphoribosyltransferase - chemistry Animals Crystallization Leishmania donovani Leishmania donovani - enzymology Stereoisomerism X-Ray Diffraction
Online-Zugang:	Volltext
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Beschreibung
Zusammenfassung:	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.
ISSN:	0887-3585 1097-0134
DOI:	10.1002/prot.11