By W. Antoni Kudlicki
The function of cell-free rabbit reticulocyte expression structures in practical proteomics / Michele Arduengo, Elaine Schenborn, and Robin Hurst -- Advances in Insect-based cell-free protein expression / Uritza von Groll ... [et al.] -- benefits and functions of the batch-formatted E. coli cell-free expression approach / Julia E. Fletcher ... [et al.] -- Energetics in Escherichia coli-based batch cell-Free structures / Kalavathy Sitaraman and Deb ok. Chatterjee -- Disulfide bond formation in bacteria-based cell-free protein expression / Aaron R. Goerke and James R. Swartz -- The natural procedure: a minimum cell-free translation procedure / Bei-Wen Ying, Yoshihiro Shimizu and Takuya Ueda -- Cell-free expression methods for the construction and characterization of membrane proteins / Daniel Schwarz ... [et al.] -- Cell-free expression for protein NMR / A.J. Shaka -- Cell-free synthesis of membrane proteins for X-ray crystallography / Julia E. Fletcher ... [et al.] --, Bacterial cell-free expression platforms for high-throughput protein creation / T.V.S. Murthy, Leonardo Brizuela, and Joshua LaBaer -- Cell-free protein synthesis for protein microarrays / Gregory A. Michaud ... [et al.] -- Cell-free protein expression screening and protein immobilization utilizing protein microarrays / Matthew A. Coleman ... [et al.] -- Cell-free protein expression labeling with fluorophores / Jerzy Olejnik -- Cell-free synthesis of outlined protein conjugates through site-directed cotranslational labeling / Michael Gerrits ... [et al.] -- C-terminal labeling of proteins utilizing fluorescently conjugated puromycin derivatives / Ichiro Tabuchi -- Translation engineering and artificial biology / David A. Roth, Liza S.Z. Larsen and G. Wesley Hatfield -- sped up protein evolution utilizing ribosome show / Julie Douthwaite, Lutz Jermutus, Ronald Jackson -- program of in vitro virus
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Extra resources for Cell-Free Protein Expression
3A, insert). Up to 40 μg active luciferase per ml reaction volume can be expressed as determined by a microtiter-based activity assay (Fig. 3A). The ability of the system to generate proteins capable of forming a protein complex was analysed in a pull-down assay with TFIIA subunits αβ and γ. Both subunits are expressed soluble in the Insect II extract (Fig. 2). For the pull-down assay, TFIIAγ was synthesized in a double-tagged form carrying a N-terminal Strep tag II and a C-terminal 6xHis tag. TFIIAαβ was N-terminally 6xHis-tagged.
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112. Cohen HM, Tawfik DS, Griffiths AD. Altering the sequence specificity of Hae III methyltransferase by directed evolution using in vitro compartmentalization. Protein Eng Des Sel 2004; 17:3-11. 113. Doi N, Kumadaki S, Oishi Y et al. In vitro selection of restriction endonucleases by in vitro compartmentalization. Nucl Acids Res 2004; 32:e95. 114. Ghadessy FJ, Holliger P. A novel emulsion mixture for in vitro compartmentalization of transcription and translation in the rabbit reticulocyte system.