Table S1.
RSFPs | Abs, nm | Emi, nm | QY | ε-max, M–1·cm−1 | Brightness | Contrast ratio* | M,† kDa | On-to-off switching half-time,‡ s |
Skylan-S | 499 | 511 | 0.64 | 152,408 | 98,029 | 18.3 | 23.8 | 4.77 |
Skylan-NS | 499 | 511 | 0.59 | 133,770 | 78,924 | 34.2 | 27.4 | 0.15 |
The absorption maximum (Abs), maximum emission (Emi), quantum yield (QY), and extinction coefficient (ε-max) were measured in PBS (pH 7.4) for the on states of the proteins.
The contrast ratio was the mean value averaged from the first 10 switching cycles in Fig. S1 B and C measured from E. coli. The value for each cycle was calculated by integrating across all pixels and all time points, the total available signal after 405 nm illumination and subtraction of the off state background, until said signal dropped to 1/e intensity of the first sampling point.
The molecular mass (M) was measured via sedimentation equilibrium.
The on-to-off switching speed was measured based on dynamics changes of fluorescence in Fig. S1 B and C.