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Optimizing E. coli-Based Membrane Protein Production Using Lemo21(DE3) and GFP-Fusions
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
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2013 (English)In: Membrane Biogenesis: Methods and Protocols / [ed] Doron Rapaport, Johannes M. Herrmann, Totowa, USA: Humana Press, 2013, 381-400 p.Chapter 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. 381-400 p.
Series
Methods in Molecular Biology, ISSN 1064-3745 ; 1033
Keyword [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: diva2:663662
Note

AuthorCount:7

Available from: 2013-11-12 Created: 2013-11-11 Last updated: 2015-11-18Bibliographically approved

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Hjelm, AnnaSchlegel, SusanBaumgarten, ThomasWickström, DavidDrew, Davidde Gier, Jan-Willem
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