. Author manuscript; available in PMC: 2016 Nov 6.

Published in final edited form as: J Mol Biol. 2015 Jul 18;427(22):3491–3500. doi: 10.1016/j.jmb.2015.07.010

Table 1.

Equilibrium binding constant for RNA and Hfq

Hfq variants	K_D1 (μM)		DsrAΔU6
Hfq variants	D16-FAM	DsrA sRNA	DsrAΔU6
WT	0.067 ± 0.005	0.22 ± 0.015	1.31 ± 0.1
D9A	0.047 ± 0.002	0.46 ± 0.018	0.67 ± 0.022
E18A	0.024 ± 0.004	0.38 ± 0.02	ND
E37A	ND	0.51 ± 0.021	ND

Overall dissociation constants per Hfq monomer were measured by fluorescence anisotropy (D16-FAM) or native gel mobility shift (DsrA and DsrAΔU6) at 30 °C in TNK buffer. ND, not done. Values are the average and standard deviation from the mean of three independent experiments. The K_d for D16-FAM and WT Hfq is about half that reported for earlier preparations of the protein ¹⁸.