title: Towards the crystal structure elucidation of eukaryotic UDP-galactopyranose mutase.
abstract: UDP-galactopyranose mutase (UGM) catalyzes the interconversion of UDP-galactopyranose and UDP-galactofuranose. Eukaryotic UGMs from Aspergillus fumigatus and Leishmania major have been purified to homogeneity by means of Ni(2+)-affinity chromatography and crystallized. Eukaryotic UGM structure elucidation was not straightforward owing to high pseudo-symmetry, twinning and very low anomalous signal. Phasing to 2.8 Å resolution using SAD was successful for L. major UGM. However, the maps could only be improved by iterative density modification and manual model building. High pseudo-symmetry and twinning prevented correct space-group assignment and the completion of structure refinement. The structure of A. fumigatus UGM to 2.52 Å resolution was determined by molecular replacement using the incomplete 2.8 Å resolution L. major UGM model.
authors.affiliation: Department of Chemistry, University of Saskatchewan, 110 Science Place, Saskatoon, Saskatchewan S7N 5C9, Canada.
authors.forename: Karin E
authors.initials: KE
authors.lastname: van Straaten
authors.forename: Francoise H
authors.initials: FH
authors.lastname: Routier
authors.forename: David A R
authors.initials: DA
authors.lastname: Sanders
mesh_terms: D001232:Aspergillus fumigatus / Q000201:enzymology*; D018360:Crystallography, X-Ray; D019751:Intramolecular Transferases / Q000737:chemistry*; D018320:Leishmania major / Q000201:enzymology*
chemical_list: D019751:Intramolecular Transferases; C098051:UDP-galactopyranose mutase