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Production of Human Norovirus Protruding Domains in E. coli for X-ray Crystallography
 

Production of Human Norovirus Protruding Domains in E. coli for X-ray Crystallography

Article DOI: 10.3791/53845-v • 10:46 min • April 19th, 2016
April 19th, 2016 •
1,2, 1,2, 1,2, 1,2
1Schaller Research Group, University of Heidelberg and the German Cancer Research Center, 2Department of Infectious Diseases, Virology, University of Heidelberg

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요약
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Here, we describe a method to express and purify high quality norovirus protruding (P) domains in E. coli for use in X-ray crystallography studies. This method can be applied to other calicivirus P domains, as well as non-structural proteins, i.e., viral protein genome-linked (VPg), protease, and RNA dependent RNA polymerase (RdRp).

Tags

Production Human Norovirus Protruding Domains E. Coli X-ray Crystallography Protein Expression Purification Crystallization Pure Protein Fast Protocol Structural Proteins Nonstructural Proteins High Resolution Adjustment Less Soluble Proteins Growth Medium Growth Temperature Transformation Protocol PMalc2x Vector MBP-His-P Domain Fusion Protein Competent E.coli BL21 Cells SOC Medium LB-ampicillin Optical Density Shaking Speed
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