Difference between revisions of "Part:BBa K1896001:Design"
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===References=== | ===References=== | ||
− | + | von Stetten, D., Noirclerc-Savoye, M., Goedhart, J., Gadella, T. W., & Royant, A. (2012). Structure of a fluorescent protein from ''Aequorea victoria'' bearing the obligate-monomer mutation A206K. ''Acta Crystallographica Section F: Structural Biology and Crystallization Communications'', 68(8), 878-882. | |
− | + | Ito, Y., Suzuki, M., & Husimi, Y. (1999). A novel mutant of green fluorescent protein with enhanced sensitivity for microanalysis at 488 nm excitation. ''Biochemical and biophysical research communications'', 264(2), 556-560. | |
− | + | Crameri, A., Whitehorn, E. A., Tate, E., Stemmer, W. P., Crameri, A., Kitts, P. A., & Kitts, P. A. (1996). Improved green fluorescent protein by molecular evolution using. ''Nat. Biotechnol'', 14(3), 315-319. |
Revision as of 22:58, 12 October 2016
mGFPuv2
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
Design Notes
After codon optimisation, 2 BsaI sites were removed.
Source
We started from pBAD-GFPuv (GenBank: U62637.1, Clontech), applied the described mutations and codon optimised the sequence for E. coli.
References
von Stetten, D., Noirclerc-Savoye, M., Goedhart, J., Gadella, T. W., & Royant, A. (2012). Structure of a fluorescent protein from Aequorea victoria bearing the obligate-monomer mutation A206K. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 68(8), 878-882. Ito, Y., Suzuki, M., & Husimi, Y. (1999). A novel mutant of green fluorescent protein with enhanced sensitivity for microanalysis at 488 nm excitation. Biochemical and biophysical research communications, 264(2), 556-560. Crameri, A., Whitehorn, E. A., Tate, E., Stemmer, W. P., Crameri, A., Kitts, P. A., & Kitts, P. A. (1996). Improved green fluorescent protein by molecular evolution using. Nat. Biotechnol, 14(3), 315-319.