title: Crystallization and preliminary X-ray analysis of Leishmania major glyoxalase I.
abstract: 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 A. 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.
authors.affiliation: Division of Biological Chemistry and Molecular Microbiology, Wellcome Trust Biocentre, School of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland.
authors.forename: Antonio
authors.initials: A
authors.lastname: Ariza
authors.forename: Tim J
authors.initials: TJ
authors.lastname: Vickers
authors.forename: Neil
authors.initials: N
authors.lastname: Greig
authors.forename: Alan H
authors.initials: AH
authors.lastname: Fairlamb
authors.forename: Charles S
authors.initials: CS
authors.lastname: Bond
mesh_terms: D000818:Animals; D003460:Crystallization; D007791:Lactoylglutathione Lyase / Q000737:chemistry*; D018320:Leishmania major / Q000201:enzymology*; D008958:Models, Molecular; D014961:X-Ray Diffraction
chemical_list: D007791:Lactoylglutathione Lyase