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Production of Human Norovirus Protruding Domains in E. coli for X-ray Crystallography
Journal JoVE
Biologie
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Journal JoVE Biologie
Production of Human Norovirus Protruding Domains in E. coli for X-ray Crystallography
DOI:

10:46 min

April 19, 2016

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Chapitres

  • 00:05Titre
  • 00:47P Domain Expression
  • 02:251st Purification Step and Protease Cleavage
  • 05:142nd Purification Step
  • 06:283rd Purification Step
  • 07:28Crystallization of the P Domain
  • 09:01Results: Evaluation of Protein Elution
  • 09:46Conclusion

Summary

Traduction automatique

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).

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