Crystallization and preliminary X-ray analysis of Leishmania major glyoxalase I

Antonio Ariza, Tim J. Vickers, Neil Greig, Alan H. Fairlamb, Charles S. Bond (Lead / Corresponding author)

    Research output: Contribution to journalArticlepeer-review

    10 Citations (Scopus)


    Glyoxalase I (GLO1) is a putative drug target for trypanosomatids, which are pathogenic protozoa that include the causative agents of leishmaniasis. Significant sequence and functional differences between Leishmania major and human GLO1 suggest that it may make a suitable template for rational inhibitor design. L. major GLO1 was crystallized in two forms: the first is extremely disordered and does not diffract, while the second, an orthorhombic form, produces diffraction to 2.0 Å. Molecular-replacement calculations indicate that there are three GLO1 dimers in the asymmetric unit, which take up a helical arrangement with their molecular dyads arranged approximately perpendicular to the c axis. Further analysis of these data are under way.

    Original languageEnglish
    Pages (from-to)769-772
    Number of pages4
    JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
    Issue number8
    Publication statusPublished - Aug 2005

    ASJC Scopus subject areas

    • Biophysics
    • Structural Biology
    • Biochemistry
    • Genetics
    • Condensed Matter Physics


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