Crystallization of the purine salvage enzyme adenine phosphoribosyltransferase

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

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

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
Volume25
Issue number4
DOIs
StatePublished - 1996

Fingerprint

Phosphoribosyl Pyrophosphate
Adenine Phosphoribosyltransferase
Leishmania donovani
Salvaging
Adenosine Monophosphate
Crystallization
Parasites
Ligands
Crystals
Enzymes
Adenosine
Substrates
purine

Keywords

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

ASJC Scopus subject areas

  • Genetics
  • Structural Biology
  • Biochemistry

Cite this

Crystallization of the purine salvage enzyme adenine phosphoribosyltransferase. / Phillips, Cynthia L.; Ullman, Buddy; Brennan, Richard G.

In: Proteins: Structure, Function and Genetics, Vol. 25, No. 4, 1996, p. 510-513.

Research output: Contribution to journalArticle

Phillips, Cynthia L. ; Ullman, Buddy ; Brennan, Richard G. / Crystallization of the purine salvage enzyme adenine phosphoribosyltransferase. In: Proteins: Structure, Function and Genetics. 1996 ; Vol. 25, No. 4. pp. 510-513.
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