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 |
Funding
We are grateful to Robert Stevens of the Mass Spectrometry Facility of the Duke University Medical Center for the ES-MS data and to Astrid Guerra for technical assistance. This project was granted synchrotron beamline access (program proposal number 4A16) by the Stanford Synchrotron Radiation Laboratory (SSRL), which is funded by the DOE and NIH. This work was supported in part by NIH Grants AI38919 (to A.E.E.), AI34326 (to S.P.C. III) and RR03051. R.N.-A. was supported by a fellowship from the Ford Foundation.
Keywords
- Crystallization
- Electro-spray mass spectrometry
- Hypoxanthine phosphoribosyltransferase
- Limited proteolysis
- Parasite
- Trypanosoma
ASJC Scopus subject areas
- Molecular Biology
- Structural Biology
- Biophysics
- Biochemistry