Aspergillus fumigatus UDP-galactopyranose mutase (AfUGM) is a potential drug target involved in the synthesis of the cell wall of this fungal pathogen. AfUGM was recombinantly produced in Escherichia coli, purified and crystallized by the sitting-drop method, producing orthorhombic crystals that diffracted to a resolution of 3.25 Å. The crystals contained four molecules per asymmetric unit and belonged to space group P2 2 2 , with unit-cell parameters a = 127.72, b = 134.30, c = 173.84 Å. Incorporation of selenomethionine was achieved, but the resulting crystals did not allow solution of the phase problem.
|Number of pages||4|
|Journal||Acta Crystallographica F-Structural Biology and Crystallization Communications|
|Publication status||Published - 2012|
Penman, G. A., Lockhart, D. E. A., Ferenbach, A., & Van Aalten, D. M. F. (2012). Purification, crystallization and preliminary X-ray diffraction data of UDP-galactopyranose mutase from Aspergillus fumigatus. Acta Crystallographica F-Structural Biology and Crystallization Communications, 68(6), 705-708. https://doi.org/10.1107/S1744309112017915