Limited proteolysis of a trypanosomal hypoxanthine phosphoribosyltransferase yields crystals that diffract X-rays to near atomic resolution

René Nieves-Alicea, Pamela J. Focia, Sydney P. Craig, Ann E. Eakin*

*Corresponding author for this work

Research output: Contribution to journalArticle

6 Scopus citations

Abstract

Two crystal forms of the hypoxanthine phosphoribosyltransferase from Trypanosoma cruzi were grown and characterized. Proteolytic modification at the C-terminus of the recombinant enzyme yielded monoclinic crystals that diffract X-rays to higher resolution than the original, trigonal crystal form. Data from the monoclinic crystal form enabled determination of the crystal structure for the trypanosomal HPRT to 1.4 A resolution. Copyright (C) 1998 Elsevier Science B.V.

Original languageEnglish (US)
Pages (from-to)500-505
Number of pages6
JournalBiochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
Volume1388
Issue number2
DOIs
StatePublished - Nov 10 1998

Keywords

  • Crystallization
  • Electro-spray mass spectrometry
  • Hypoxanthine phosphoribosyltransferase
  • Limited proteolysis
  • Parasite
  • Trypanosoma

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology

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