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- W2939846670 abstract "Escherichia coli (E. coli) is the most widely used expression host for recombinant proteins due to high expression yields and straightforward molecular cloning. Directed evolution of G protein-coupled receptors (GPCRs) has made several of these difficult to express membrane proteins amenable to prokaryotic expression. Here, we describe a protocol for near complete 13CH3-methionine labeling of a thermostable neurotensin receptor 1 (enNTS1) variant in E. coli for solution NMR-based dynamics studies. Our expression strategy utilizes methionine biosynthesis pathway inhibition forcing E. coli to incorporate exogenous methionine with 96% efficiency at expression levels of 2.6 mg enNTS1 per liter of expression culture containing 50 mg of 13CH3-methionine. We also provide a 3-step purification protocol that produces final yields of 0.6 mg of functional Apo-state enNTS1." @default.
- W2939846670 created "2019-04-25" @default.
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- W2939846670 creator A5088336824 @default.
- W2939846670 date "2019-01-01" @default.
- W2939846670 modified "2023-09-27" @default.
- W2939846670 title "Expression and Purification of a Functional E. coli 13CH3-Methionine-Labeled Thermostable Neurotensin Receptor 1 Variant for Solution NMR Studies" @default.
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- W2939846670 doi "https://doi.org/10.1007/978-1-4939-9121-1_3" @default.
- W2939846670 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30969410" @default.
- W2939846670 hasPublicationYear "2019" @default.
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