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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.

SUBMITTER: van Straaten KE 

PROVIDER: S-EPMC3325819 | biostudies-literature | 2012 Apr

REPOSITORIES: biostudies-literature

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Towards the crystal structure elucidation of eukaryotic UDP-galactopyranose mutase.

van Straaten Karin E KE   Routier Francoise H FH   Sanders David A R DA  

Acta crystallographica. Section F, Structural biology and crystallization communications 20120328 Pt 4


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 onl  ...[more]

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