ArticleJournal of biomolecular NMR2012
High-yield Escherichia coli-based cell-free expression of human proteins.
Article in Journal of biomolecular NMR, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 27 citations in OpenAlex.
- Applications of cell free protein synthesis in protein design.Protein science : a publication of the Protein Society · 2024Review
- Unexpected dynamics in femtomolar complexes of binding proteins with peptides.Nature communications · 2023Article
- Nucleotide-amino acid π-stacking interactions initiate photo cross-linking in RNA-protein complexes.Nature communications · 2022Article
- An automated iterative approach for protein structure refinement using pseudocontact shifts.Journal of biomolecular NMR · 2021Article
- MINA-1 and WAGO-4 are part of regulatory network coordinating germ cell death and RNAi in C. elegans.Cell death and differentiation · 2019Article
- Molecular basis for disassembly of an importin:ribosomal protein complex by the escortin Tsr2.Nature communications · 2018Article
- Molecular cloning and expression of high GC-rich novel tumor suppressor gene HIC-1.Molecular biotechnology · 2014Article
- Article
- Molecular basis for the wide range of affinity found in Csr/Rsm protein-RNA recognition.Nucleic acids research · 2014Article
- N-terminal fusion tags for effective production of g-protein-coupled receptors in bacterial cell-free systems.Acta naturae · 2012Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Production of sufficient amounts of human proteins is a frequent bottleneck in structural biology. Here we describe an Escherichia coli-based cell-free system which yields mg-quantities of human proteins in N-terminal fusion constructs with the GB1 domain, which show significantly increased translation efficiency. A newly generated E. coli BL21 (DE3) RIPL-Star strain was used, which contains a variant RNase E with reduced activity and an excess of rare-codon tRNAs, and is devoid of lon and ompT protease activity. In the implementation of the expression system we used freshly in-house prepared cell extract. Batch-mode cell-free expression with this setup was up to twofold more economical than continuous-exchange expression, with yields of 0.2-0.9 mg of purified protein per mL of reaction mixture. Native folding of the proteins thus obtained is documented with 2D [(15)N,(1)H]-HSQC NMR.
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