| Oligomerization | Organism | Molecular Weight | Cofactor |
|---|---|---|---|
| Monomer | Aequorea victoria | 26.9 kDa | - |
| Ex λ | Em λ | EC (M-1 cm-1) | QY | Brightness | pKa | Maturation (min) | Lifetime (ns) |
|---|---|---|---|---|---|---|---|
| 379 | 446 | 41,000 | 0.45 | 18.45 | 6.6 |
No photostability measurements available ... add one!
EBFP1.2 was derived from EBFP with the following mutations: S30R/Y39N/T65S/S72A/N105T/I171V/N198S/A206V
amino acid numbers relative to avGFP. show relative to EBFP
We had initially presumed that EBFP was close to the maximum achievable fluorescent brightness for its particular chromophore structure. However, the recent report from Waldo and co-workers that introduction of the “superfolder” mutations into BFP improved the fluorescent brightness in bacterial colonies galvanized us to explore whether these mutations could also benefit EBFP. Mutations S30R/Y39N/T65S/S72A/N105T/I171V/N198S/A206V were introduced into EBFP by site-directed mutagenesis to produce EBFP1.2
Ai et al. (2007)
(2007). Biochemistry, 46(20) , 5904-5910. doi: 10.1021/bi700199g. Article Pubmed
(2011). Nature Methods, 8(5) , 393-399. doi: 10.1038/nmeth.1596. Article Pubmed
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