Table 3.

EXAFS fitting results for dicobalt AHL lactonase.^a

Fit	Scatterer(b)	Path(c)	Ras (Å)	σas2(d)	Rf(e)	Ru(e)
1	5 N/O		2.03	7.2	27	267
2	5 N/O		2.03	6.0	199	201
	2 His	C1	2.98	9.0
		C1-N1	3.35	6.0
		C2-N1	4.22	15.
		C1-N2-N1	4.67	14.
3	5 N/O		2.03	6.0	146	157
	2 His	C1	3.02	6.4
		C1-N1	3.38	16.
		C2-N1	4.24	6.6
		C1-N2-N1	4.68	13.
	1 Co	Co	3.55	9.0

^aValues of R_as and σ_as² are for fits to filtered data, as described in Materials and Methods. Fits to unfiltered data gave similar results.

^bInteger coordination number giving the best fit.

^cMultiple scattering paths represent combined paths, with labels that correspond to the path with largest amplitude (19).

^dMean square deviation in absorber-scatterer bond length in 10⁻³ Ų.

^eGoodness of fit defined as 1000*$\frac{{\displaystyle \sum _{i=1}^N\left\{{\left[\mathrm{Re}({\chi }_{i_{calc}})\right]}^2+{\left[\mathrm{Im}({\chi }_{i_{calc}})\right]}^2\right\}}}{{\displaystyle \sum _{i=1}^N\left\{{\left[\mathrm{Re}({\chi }_{i_{obs}})\right]}^2+{\left[\mathrm{Im}({\chi }_{i_{obs}})\right]}^2\right\}}}$, where N is the number of data points. Rf corresponds to fits to filtered data, Ru corresponds to fits to unfiltered data. The apparent similarity of the residuals for filtered and unfiltered fits is an artifact of the Fourier filtering process, which converts real data (unfiltered) into complex data (filtered). This results in an effective doubling of the number of points being fit, leading to apparently higher residuals for fits to filtered data.