Table 1. Sedimentation and Photophysical Parameters of Different Fluorescent Proteins as a Function of Laser Power^a.

molecule	rotor speed	power (mW)	signal/rmsd ratio	rate (1/h)	spatial drift (%/cm)	s (S)	f/f0c
Dronpa	50 000	50.2	480	0.257 (0.250–0.265)	7.1 (6.3–7.9)	2.75	1.31
	50 000	8.4	320	0.030d (0.028–0.032)d	3.4 (2.6–4.0)d	2.74	1.31
	50 000	2.1	260	0 (<0.004)d	2.5	2.77	1.30
	3000	50.2		0.219
Padron	50 000	50.2	114	1.46 (1.37–1.53)	0.7 (−1.1–2.8)	2.64	1.25
	50 000	8.4	90	0.29 (0.16–0.45)	10.6 (−13–43)	2.58	1.25
	50 000	2.1	14.4	0.038	9.9	2.68	1.34
	3000	50.2		1.43
EGFP pH 7.4, PBS	50 000	50.2	222	0.86% (0.4–1.1)	9.4 (7–14)	2.72	1.40
	50 000	8.4	84	0.21% (−0.1–1.1)	11.4 (6–18)	2.71	1.45
	50 000	2.1	64	0.74%	6.8	2.75	1.38
EGFPe pH 5.7, ce6	50 000	50.2	289	0.52%b (0.3–0.8)	11.9 (9–15)	2.72	1.37

^aAll samples at the same laser power and rotor speed were measured side-by-side in the same run. All protein concentrations are 100 nM. Error intervals calculated by F-statistics on a 68% confidence interval.

^b%/hour linear drift.

^cUncorrected for solvent buoyancy, viscosity, and protein partial-specific volume.

^dWith A constrained to zero (limit of complete photobleaching) to avoid correlation with the rate.

^eIn the presence of 100 μM chlorin e₆, phosphate buffered saline at pH 5.7.