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Overexpression and purification of U24 from human herpesvirus type-6 in E. coli: unconventional use of oxidizing environments with a maltose binding protein-hexahistine dual tag to enhance membrane protein yield
BACKGROUND: Obtaining membrane proteins in sufficient quantity for biophysical study and biotechnological applications has been a difficult task. Use of the maltose binding protein/hexahistidine dual tag system with E.coli as an expression host is emerging as a high throughput method to enhance memb...
| Autores principales: | , |
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| Formato: | Online Artículo Texto |
| Lenguaje: | English |
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BioMed Central
2011
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| Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3155487/ https://www.ncbi.nlm.nih.gov/pubmed/21714924 http://dx.doi.org/10.1186/1475-2859-10-51 |