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. Author manuscript; available in PMC: 2015 Apr 16.

Published in final edited form as: Nat Commun. 2014;5:3282. doi: 10.1038/ncomms4282

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a, β-Galactosidase expression in E. coli cells co-expressing histidine kinase KdpD with wild-type KdpE, KdpE-E216A, double substituent KdpE-E216A-D52A, or inactive KdpE-D52A and KdpE-D52E in inducing media without K⁺ () or in 10 mM K⁺ (). b, Analysis of binding of KdpE (black circles) and KdpE-E216A (white circles) to DNA by fluorescence anisotropy; estimated dissociation constants were 30 ± 4.0 nM and 3.5 ± 0.5 nM, respectively. Error bars represent SEM of three independent measurements. c and d, Surface plasmon resonance analysis. The binding to DNA immobilized on a chip was analyzed by injecting various concentrations of (c) KdpE (50 – 300 nM) and (d) KdpE-E216A (10 – 50 nM).

Inline graphic — a, β-Galactosidase expression in E. coli cells co-expressing histidine kinase KdpD with wild-type KdpE, KdpE-E216A, double substituent KdpE-E216A-D52A, or inactive KdpE-D52A and KdpE-D52E in inducing media without K⁺ () or in 10 mM K⁺ (). b, Analysis of binding of KdpE (black circles) and KdpE-E216A (white circles) to DNA by fluorescence anisotropy; estimated dissociation constants were 30 ± 4.0 nM and 3.5 ± 0.5 nM, respectively. Error bars represent SEM of three independent measurements. c and d, Surface plasmon resonance analysis. The binding to DNA immobilized on a chip was analyzed by injecting various concentrations of (c) KdpE (50 – 300 nM) and (d) KdpE-E216A (10 – 50 nM).