Towards the crystal structure elucidation of eukaryotic UDP-galactopyranose mutase.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 68(Pt 4): 455-9, 2012 Apr 01.
Article
en En
| MEDLINE
| ID: mdl-22505419
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.
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1
Bases de datos:
MEDLINE
Asunto principal:
Aspergillus fumigatus
/
Leishmania major
/
Transferasas Intramoleculares
Idioma:
En
Revista:
Acta Crystallogr Sect F Struct Biol Cryst Commun
Año:
2012
Tipo del documento:
Article
País de afiliación:
Canadá