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Crystallization of quinoprotein glucose dehydrogenase variants and homologues by microseeding
The soluble quinoprotein glucose dehydrogenase oxidizes glucose, maltose and a variety of other monosaccharides and disaccharides to the corresponding lactones. An efficient microseeding protocol is reported to produce crystals of three variants that display reduced activity towards maltose. Similar...
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Formato: | Texto |
Lenguaje: | English |
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International Union of Crystallography
2006
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2243101/ https://www.ncbi.nlm.nih.gov/pubmed/16754970 http://dx.doi.org/10.1107/S1744309106014862 |
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author | Sanchez-Weatherby, Juan Southall, Stacey Oubrie, Arthur |
author_facet | Sanchez-Weatherby, Juan Southall, Stacey Oubrie, Arthur |
author_sort | Sanchez-Weatherby, Juan |
collection | PubMed |
description | The soluble quinoprotein glucose dehydrogenase oxidizes glucose, maltose and a variety of other monosaccharides and disaccharides to the corresponding lactones. An efficient microseeding protocol is reported to produce crystals of three variants that display reduced activity towards maltose. Similar cross-seeding protocols to grow crystals of homologues from Escherichia coli and Streptomyces coelicolor are described. |
format | Text |
id | pubmed-2243101 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2006 |
publisher | International Union of Crystallography |
record_format | MEDLINE/PubMed |
spelling | pubmed-22431012008-03-13 Crystallization of quinoprotein glucose dehydrogenase variants and homologues by microseeding Sanchez-Weatherby, Juan Southall, Stacey Oubrie, Arthur Acta Crystallogr Sect F Struct Biol Cryst Commun Crystallization Communications The soluble quinoprotein glucose dehydrogenase oxidizes glucose, maltose and a variety of other monosaccharides and disaccharides to the corresponding lactones. An efficient microseeding protocol is reported to produce crystals of three variants that display reduced activity towards maltose. Similar cross-seeding protocols to grow crystals of homologues from Escherichia coli and Streptomyces coelicolor are described. International Union of Crystallography 2006-05-05 /pmc/articles/PMC2243101/ /pubmed/16754970 http://dx.doi.org/10.1107/S1744309106014862 Text en © International Union of Crystallography 2006 http://journals.iucr.org/services/termsofuse.html This is an open-access article distributed under the terms described at http://journals.iucr.org/services/termsofuse.html. |
spellingShingle | Crystallization Communications Sanchez-Weatherby, Juan Southall, Stacey Oubrie, Arthur Crystallization of quinoprotein glucose dehydrogenase variants and homologues by microseeding |
title | Crystallization of quinoprotein glucose dehydrogenase variants and homologues by microseeding |
title_full | Crystallization of quinoprotein glucose dehydrogenase variants and homologues by microseeding |
title_fullStr | Crystallization of quinoprotein glucose dehydrogenase variants and homologues by microseeding |
title_full_unstemmed | Crystallization of quinoprotein glucose dehydrogenase variants and homologues by microseeding |
title_short | Crystallization of quinoprotein glucose dehydrogenase variants and homologues by microseeding |
title_sort | crystallization of quinoprotein glucose dehydrogenase variants and homologues by microseeding |
topic | Crystallization Communications |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2243101/ https://www.ncbi.nlm.nih.gov/pubmed/16754970 http://dx.doi.org/10.1107/S1744309106014862 |
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