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...

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Detalles Bibliográficos
Autores principales: Tait, Andrew R, Straus, Suzana K
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2011
Materias:
Research
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

Internet

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

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