Difference between revisions of "Part:BBa K1896008:Design"

 
 
Line 18: Line 18:
  
 
===References===
 
===References===
 +
# Green, R. L., Corotto, L. V., & Warren, G. J. (1988). Deletion mutagenesis of the ice nucleation gene from ''Pseudomonas syringae S203''. ''Molecular and General Genetics MGG'', 215(1), 165-172.
 +
# Li, L., Gyun Kang, D., & Joon Cha, H. (2004). Functional display of foreign protein on surface of ''Escherichia coli'' using N‐terminal domain of ice nucleation protein. ''Biotechnology and bioengineering'', 85(2), 214-221.

Latest revision as of 18:24, 13 October 2016


INP_RC


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal NgoMIV site found at 142
    Illegal NgoMIV site found at 1654
    Illegal NgoMIV site found at 1798
    Illegal NgoMIV site found at 2062
    Illegal NgoMIV site found at 2206
    Illegal NgoMIV site found at 2254
    Illegal NgoMIV site found at 2374
    Illegal AgeI site found at 1318
  • 1000
    COMPATIBLE WITH RFC[1000]


Design Notes

The repeat domain in this part seems to be impossible to create synthetically so PCR was used instead, with primers binding just outside of the repeat region. The absence of a stop codon allows for seamless assembly of fusion proteins.



Source

Part:BBa_K1896001


References

  1. Green, R. L., Corotto, L. V., & Warren, G. J. (1988). Deletion mutagenesis of the ice nucleation gene from Pseudomonas syringae S203. Molecular and General Genetics MGG, 215(1), 165-172.
  2. Li, L., Gyun Kang, D., & Joon Cha, H. (2004). Functional display of foreign protein on surface of Escherichia coli using N‐terminal domain of ice nucleation protein. Biotechnology and bioengineering, 85(2), 214-221.