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

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 dif...

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Autores principales: Penman, George A., Lockhart, Deborah E. A., Ferenbach, Andrew, van Aalten, Daan M. F.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3370916/
https://www.ncbi.nlm.nih.gov/pubmed/22684076
http://dx.doi.org/10.1107/S1744309112017915
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author Penman, George A.
Lockhart, Deborah E. A.
Ferenbach, Andrew
van Aalten, Daan M. F.
author_facet Penman, George A.
Lockhart, Deborah E. A.
Ferenbach, Andrew
van Aalten, Daan M. F.
author_sort Penman, George A.
collection PubMed
description 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(1)2(1)2(1), 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.
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spelling pubmed-33709162012-06-11 Purification, crystallization and preliminary X-ray diffraction data of UDP-galactopyranose mutase from Aspergillus fumigatus Penman, George A. Lockhart, Deborah E. A. Ferenbach, Andrew van Aalten, Daan M. F. Acta Crystallogr Sect F Struct Biol Cryst Commun Crystallization Communications 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(1)2(1)2(1), 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. International Union of Crystallography 2012-05-23 /pmc/articles/PMC3370916/ /pubmed/22684076 http://dx.doi.org/10.1107/S1744309112017915 Text en © Penman et al. 2012 http://creativecommons.org/licenses/by/2.0/uk/ This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.
spellingShingle Crystallization Communications
Penman, George A.
Lockhart, Deborah E. A.
Ferenbach, Andrew
van Aalten, Daan M. F.
Purification, crystallization and preliminary X-ray diffraction data of UDP-galactopyranose mutase from Aspergillus fumigatus
title Purification, crystallization and preliminary X-ray diffraction data of UDP-galactopyranose mutase from Aspergillus fumigatus
title_full Purification, crystallization and preliminary X-ray diffraction data of UDP-galactopyranose mutase from Aspergillus fumigatus
title_fullStr Purification, crystallization and preliminary X-ray diffraction data of UDP-galactopyranose mutase from Aspergillus fumigatus
title_full_unstemmed Purification, crystallization and preliminary X-ray diffraction data of UDP-galactopyranose mutase from Aspergillus fumigatus
title_short Purification, crystallization and preliminary X-ray diffraction data of UDP-galactopyranose mutase from Aspergillus fumigatus
title_sort purification, crystallization and preliminary x-ray diffraction data of udp-galactopyranose mutase from aspergillus fumigatus
topic Crystallization Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3370916/
https://www.ncbi.nlm.nih.gov/pubmed/22684076
http://dx.doi.org/10.1107/S1744309112017915
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