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. Author manuscript; available in PMC: 2011 Oct 19.
Published in final edited form as: Biochemistry. 2010 Oct 19;49(41):8818–8830. doi: 10.1021/bi100557v

Table 1.

Equilibrium dissociation constants for 1µM wild type SgrAI dimer and DNA sequences at 4°C.

DNAa Bufferb KDc (nM)
FPA		 KDc (nM)
Gel shift
18-1 1 2.5±0.9 0.6±0.2
18-2 1 1.5±0.2 2.6±1.2
40-1 1 0.9±0.2 0.057±0.009
PCP 1 6±2 ND
PC 1 5±1 ND
PCP 2 3±1 ND
PCP 3 14±4 ND
a

FPA utilized HEX labeled 18-1, 40-1, 18-2 and FLO labeled PCP, and PC.

b

Buffer 1: 20 mM Tris-Acetate (pH 8.0), 50 mM KOAc, 10 mM Ca(OAc)2, 1 mM DTT, 10% glycerol.

Buffer 2: 20 mM Tris-Acetate (pH 8.0), 50 mM KOAc, 10 mM Ca(OAc) 2, 1 mM DTT.

Buffer 3: 20 mM Tris-Acetate (pH 8.0), 50 mM KOAc, 10 mM Mg(OAc) 2, 1 mM DTT.

c

Equilibrium dissociation constants, KD given as the average of at least three different measurements ± the standard deviation, and assuming 1:1 binding.