Abstract
Recombinant tryparedoxin, a thioredoxin homologue from Crithidia fasciculata, has been purified from an Escherichia coli expression system and used in crystallization trials. Orthorhombic needles in space group P212121, with unit cell dimensions of a = 38.63, b = 51.47, and c = 73.41 Å, have been obtained. The crystals present a monomer of approximate molecular mass 16 kDa in the asymmetric unit and diffract to 1.8-Å resolution using synchrotron radiation. Structure determination will be carried out to further the understanding of the role tryparedoxin plays in regulating oxidative stress in parasitic trypanosomatids.
Original language | English |
---|---|
Pages (from-to) | 76-79 |
Number of pages | 4 |
Journal | Journal of Structural Biology |
Volume | 126 |
Issue number | 1 |
DOIs | |
Publication status | Published - 1 Jun 1999 |
Keywords
- Crithidia fasciculata
- Crystallization
- Thioredoxin
- Tryparedoxin
- X-ray diffraction
ASJC Scopus subject areas
- Structural Biology