Crystallization of the purine salvage enzyme adenine phosphoribosyltransferase

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

Research output: Contribution to journalArticlepeer-review

5 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)510-513
Number of pages4
JournalProteins: Structure, Function and Genetics
Issue number4
StatePublished - 1996
Externally publishedYes


  • Leishmania
  • X-ray diffraction
  • parasite metabolism
  • selenomethionine

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Biology


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