We are analyzing https://link.springer.com/protocol/10.1007/978-1-62703-691-7_2.

Title:
Stable Expression Clones and Auto-Induction for Protein Production in E. coli | SpringerLink
Description:
Inducible production of proteins from cloned genes in E. coli is widely used, economical, and effective. However, common practices can result in unintended induction, inadvertently generating cultures that give poor or variable yields in protein production. Recipes...
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Keywords {🔍}

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Topics {✒️}

month download article/chapter spontaneous camp-dependent derepression high-density shaking cultures stable expression clones protocol structural genomics suitable auto-inducing medium internal research funding privacy choices/manage cookies t7 expression system device instant download fully inducible cells studier fw t7 rna polymerase inducible expression systems structural genomics bacteriophage t7 lysozyme controlling basal expression recombinant expression instability author information authors inadvertently generating cultures expression strains grow assuring high yields european economic area x-ray crystallography dubendorff jw stationary phase plays general medical sciences target t7 promoter journal finder publish protocol studier conditions privacy policy brookhaven national laboratory protein structure initiative late log phase monitoring culture growth recombinant protein production accepting optional cookies main content log saturation generally produces direct expression environmental research defined culture media protocol usd 49 chapter log stable isotopes permissions reprints inducible cells protocol cite cell density humana press

Schema {🗺️}

ScholarlyArticle:
      headline:Stable Expression Clones and Auto-Induction for Protein Production in E. coli
      pageEnd:32
      pageStart:17
      image:https://media.springernature.com/w153/springer-static/cover/book/978-1-62703-691-7.jpg
      genre:
         Springer Protocols
      isPartOf:
         name:Structural Genomics
         isbn:
            978-1-62703-691-7
            978-1-62703-690-0
         type:Book
      publisher:
         name:Humana Press
         logo:
            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
         type:Organization
      author:
            name:F. William Studier
            affiliation:
                  name:Brookhaven National Laboratory
                  address:
                     name:Biosciences Department, Brookhaven National Laboratory, Upton, USA
                     type:PostalAddress
                  type:Organization
            type:Person
      keywords:Auto-induction, T7 expression system, Stable inducible cultures, Protein production, Protein labeling
      description:Inducible production of proteins from cloned genes in E. coli is widely used, economical, and effective. However, common practices can result in unintended induction, inadvertently generating cultures that give poor or variable yields in protein production. Recipes are provided for (1) defined culture media in which expression strains grow to saturation without induction, thereby ensuring stable frozen stocks and seed cultures with high fractions of fully inducible cells, and (2) defined or complex media that maintain the same high fraction of inducible cells until auto-induction in late log phase to produce fully induced high-density cultures at saturation. Simply inoculating a suitable auto-inducing medium from such a seed culture and growing to saturation generally produces much higher levels of target protein per volume of culture than monitoring culture growth and adding IPTG or other inducer at the appropriate cell density. Many strains may be conveniently screened in parallel, and burdensome inoculation with fresh colonies, sometimes employed in hopes of assuring high yields, is entirely unnecessary. These media were developed for the T7 expression system using pET vectors in BL21(DE3) but are suitable or adaptable for other inducible expression systems in E. coli and for labeling proteins with selenomethionine for X-ray crystallography or with stable isotopes for NMR.
      datePublished:2014
      isAccessibleForFree:
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         type:WebPageElement
      context:https://schema.org
Book:
      name:Structural Genomics
      isbn:
         978-1-62703-691-7
         978-1-62703-690-0
Organization:
      name:Humana Press
      logo:
         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:Brookhaven National Laboratory
      address:
         name:Biosciences Department, Brookhaven National Laboratory, Upton, USA
         type:PostalAddress
ImageObject:
      url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
Person:
      name:F. William Studier
      affiliation:
            name:Brookhaven National Laboratory
            address:
               name:Biosciences Department, Brookhaven National Laboratory, Upton, USA
               type:PostalAddress
            type:Organization
PostalAddress:
      name:Biosciences Department, Brookhaven National Laboratory, Upton, USA
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