Optimizing E. coli-Based Membrane Protein Production Using Lemo21(DE3) and GFP-FusionsShow others and affiliations
2013 (English)In: Membrane Biogenesis: Methods and Protocols / [ed] Doron Rapaport, Johannes M. Herrmann, Totowa, USA: Humana Press, 2013, p. 381-400Chapter in book (Refereed)
Abstract [en]
Optimizing the conditions for the overexpression of membrane proteins in E. coli and their subsequent purification is usually a laborious and time-consuming process. Combining the Lemo21(DE3) strain, which conveniently allows to identify the optimal expression intensity of a membrane protein using only one strain, and membrane proteins C-terminally fused to Green Fluorescent Protein (GFP) greatly facilitates the production of high-quality membrane protein material for functional and structural studies.
Place, publisher, year, edition, pages
Totowa, USA: Humana Press, 2013. p. 381-400
Series
Methods in Molecular Biology, ISSN 1064-3745 ; 1033
Keywords [en]
Membrane protein, Overexpression, Purification, E. coli, Lemo21(DE3), Fluorescence, GFP, FSEC
National Category
Cell Biology
Research subject
Biochemistry
Identifiers
URN: urn:nbn:se:su:diva-96139DOI: 10.1007/978-1-62703-487-6_24ISI: 000325643800025ISBN: 978-1-62703-486-9 (print)ISBN: 978-1-62703-487-6 (print)OAI: oai:DiVA.org:su-96139DiVA, id: diva2:663662
Note
AuthorCount:7
2013-11-122013-11-112022-02-24Bibliographically approved