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International Union of Crystallography, Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 6(68), p. 705-708, 2012

DOI: 10.1107/s1744309112017915

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Purification, crystallization and preliminary X-ray diffraction data of UDP-galactopyranose mutase fromAspergillus fumigatus

Journal article published in 2012 by George A. Penman, Deborah E. A. Lockhart, Andrew Ferenbach, Daan M. F. van Aalten ORCID
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

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. © 2012 International Union of Crystallography All rights reserved.