biostudies-literature00600Unknown68(Pt 4)van Straaten KECanadian Institutes of Health ResearchUDP-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.Acta crystallographica. Section F, Structural biology and crystallization communications455-9https://www.ebi.ac.uk/biostudies/studies/S-EPMC3325819biostudies-literatureTowards the crystal structure elucidation of eukaryotic UDP-galactopyranose mutase.PMC3325819van Straaten KERoutier FHSanders DA60falseTowards the crystal structure elucidation of eukaryotic UDP-galactopyranose mutase.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.2012-01-01T00:00:00Z2012 Apr2024-11-21T01:16:42.155Z2019-03-26T22:32:11ZS-EPMC33258192250541910.1107/S174430911200691410.1107/s1744309112006914