Crystallization of recombinant Crithidia fasciculata tryparedoxin

Magnus S. Alphey, Emmanuel Tetaud, David G. Gourley, Alan H. Fairlamb, William N. Hunter (Lead / Corresponding author)

    Research output: Contribution to journalArticlepeer-review

    6 Citations (Scopus)

    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 languageEnglish
    Pages (from-to)76-79
    Number of pages4
    JournalJournal of Structural Biology
    Volume126
    Issue number1
    DOIs
    Publication statusPublished - 1 Jun 1999

    Keywords

    • Crithidia fasciculata
    • Crystallization
    • Thioredoxin
    • Tryparedoxin
    • X-ray diffraction

    ASJC Scopus subject areas

    • Structural Biology

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