(2007). Biochemistry, 46(20) , 5904-5910. doi: 10.1021/bi700199g. Article Pubmed
Protein (state) | t1/2 (s) | Power | Light | Mode | In Cell | Fusion | ˚C |
---|---|---|---|---|---|---|---|
mKalama1 | 2.5 |
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