ArticleMethods in molecular biology (Clifton, N.J.)2014
Protein production for structural genomics using E. coli expression.
Article in Methods in molecular biology (Clifton, N.J.), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
23 citing papers in PubMed, 33 citations in OpenAlex.
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- Structure of papain-like protease from SARS-CoV-2 and its complexes with non-covalent inhibitors.Nature communications · 2021Article
- Crystal structure of Nsp15 endoribonuclease NendoU from SARS-CoV-2.Protein science : a publication of the Protein Society · 2020Article
- Structural and functional characterization of three Type B and C chloramphenicol acetyltransferases from Vibrio species.Protein science : a publication of the Protein Society · 2020Article
- Optimization of culture conditions for the expression of three different insoluble proteins in Escherichia coli.Scientific reports · 2019Article
- Purification of Tag-FreeBiochemistry · 2019Article
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- Crystal structure of nonphosphorylated receiver domain of the stress response regulator RcsB from Escherichia coli.Protein science : a publication of the Protein Society · 2016Article
- Gene selection and cloning approaches for co-expression and production of recombinant protein-protein complexes.Journal of structural and functional genomics · 2015Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
The goal of structural biology is to reveal details of the molecular structure of proteins in order to understand their function and mechanism. X-ray crystallography and NMR are the two best methods for atomic level structure determination. However, these methods require milligram quantities of proteins. In this chapter a reproducible methodology for large-scale protein production applicable to a diverse set of proteins is described. The approach is based on protein expression in E. coli as a fusion with a cleavable affinity tag that was tested on over 20,000 proteins. Specifically, a protocol for fermentation of large quantities of native proteins in disposable culture vessels is presented. A modified protocol that allows for the production of selenium-labeled proteins in defined media is also offered. Finally, a method for the purification of His6-tagged proteins on immobilized metal affinity chromatography columns that generates high-purity material is described in detail.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.