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Optimizing E. coli-based membrane protein production using Lemo21(DE3) and GFP-fusions

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Optimizing E. coli-based membrane protein production using Lemo21(DE3) and GFP-fusions. / Hjelm, Anna; Schlegel, Susan; Baumgarten, Thomas; Klepsch, Mirjam; Wickström, David; Drew, David; de Gier, Jan-Willem.

In: Methods Mol Biol, Vol. 1033, 2013, p. 381-400.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Hjelm, A, Schlegel, S, Baumgarten, T, Klepsch, M, Wickström, D, Drew, D & de Gier, J-W 2013, 'Optimizing E. coli-based membrane protein production using Lemo21(DE3) and GFP-fusions', Methods Mol Biol, vol. 1033, pp. 381-400. https://doi.org/10.1007/978-1-62703-487-6_24

APA

Hjelm, A., Schlegel, S., Baumgarten, T., Klepsch, M., Wickström, D., Drew, D., & de Gier, J-W. (2013). Optimizing E. coli-based membrane protein production using Lemo21(DE3) and GFP-fusions. Methods Mol Biol, 1033, 381-400. https://doi.org/10.1007/978-1-62703-487-6_24

Vancouver

Hjelm A, Schlegel S, Baumgarten T, Klepsch M, Wickström D, Drew D et al. Optimizing E. coli-based membrane protein production using Lemo21(DE3) and GFP-fusions. Methods Mol Biol. 2013;1033:381-400. https://doi.org/10.1007/978-1-62703-487-6_24

Bibtex

@article{ca11a95f24634186a7734bbd410ed7ef,
title = "Optimizing E. coli-based membrane protein production using Lemo21(DE3) and GFP-fusions",
abstract = "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.",
keywords = "Bioreactors, Escherichia coli, Fermentation, Gene Expression Regulation, Bacterial, Genetic Vectors, Green Fluorescent Proteins, Membrane Proteins, Recombinant Fusion Proteins, Transformation, Bacterial, Journal Article, Research Support, N.I.H., Extramural, Research Support, Non-U.S. Gov't",
author = "Anna Hjelm and Susan Schlegel and Thomas Baumgarten and Mirjam Klepsch and David Wickstr{\"o}m and David Drew and {de Gier}, Jan-Willem",
year = "2013",
doi = "10.1007/978-1-62703-487-6_24",
language = "English",
volume = "1033",
pages = "381--400",
journal = "Methods Mol Biol",
issn = "1064-3745",
publisher = "Humana Press",

}

RIS

TY - JOUR

T1 - Optimizing E. coli-based membrane protein production using Lemo21(DE3) and GFP-fusions

AU - Hjelm, Anna

AU - Schlegel, Susan

AU - Baumgarten, Thomas

AU - Klepsch, Mirjam

AU - Wickström, David

AU - Drew, David

AU - de Gier, Jan-Willem

PY - 2013

Y1 - 2013

N2 - 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.

AB - 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.

KW - Bioreactors

KW - Escherichia coli

KW - Fermentation

KW - Gene Expression Regulation, Bacterial

KW - Genetic Vectors

KW - Green Fluorescent Proteins

KW - Membrane Proteins

KW - Recombinant Fusion Proteins

KW - Transformation, Bacterial

KW - Journal Article

KW - Research Support, N.I.H., Extramural

KW - Research Support, Non-U.S. Gov't

U2 - 10.1007/978-1-62703-487-6_24

DO - 10.1007/978-1-62703-487-6_24

M3 - SCORING: Journal article

C2 - 23996190

VL - 1033

SP - 381

EP - 400

JO - Methods Mol Biol

JF - Methods Mol Biol

SN - 1064-3745

ER -