| Oligomerization | Organism | Molecular Weight | Cofactor |
|---|---|---|---|
| Monomer | Aequorea victoria | 27.0 kDa | - |
| State | Ex λ | Em λ | EC (M-1 cm-1) | QY | Brightness | pKa | Maturation (min) | Lifetime (ns) |
|---|---|---|---|---|---|---|---|---|
| Off | ||||||||
| On | 493 | 510 | 47,000 | 0.36 | 16.92 | 6.5 | 180.0 |
No photostability measurements available ... add one!
rsEGFP was derived from mEGFP with the following mutations: Q69L/V150A/V163S/S205N
amino acid numbers relative to avGFP. show relative to mEGFP
We compared the properties of rsEGFP with that of the well-known RSFP Dronpa. With the proteins embedded in a 12.5% polyacrylamide layer and using light of 491 nm and 405 nm, a complete on–off cycle took 250 ms for Dronpa and 20 ms for rsEGFP. Dronpa went through <10 cycles before its fluorescence was reduced to 50%, whereas rsEGFP went through ∼1,200 cycles under the same conditions. To compare bleaching, Dronpa and rsEGFP were kept in the on-state by continuous irradiation at 405 nm while fluorescence was generated by irradiation at 491 nm. Whereas Dronpa fluorescence was reduced to 50% within t½ ≈ 30 s, for rsEGFP we measured t½ ≈ 800 s.
Grotjohann et al. (2011)
(2011). Nature, 478(7368) , 204-208. doi: 10.1038/nature10497. Article Pubmed
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