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 language | English (US) |
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Pages (from-to) | 500-505 |
Number of pages | 6 |
Journal | Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology |
Volume | 1388 |
Issue number | 2 |
DOIs | |
State | Published - Nov 10 1998 |
Keywords
- Crystallization
- Electro-spray mass spectrometry
- Hypoxanthine phosphoribosyltransferase
- Limited proteolysis
- Parasite
- Trypanosoma
ASJC Scopus subject areas
- Structural Biology
- Biophysics
- Biochemistry
- Molecular Biology