Table II.

Data Collection, Phasing, and Refinement Statistics

Dataset	Native	Selenomethionine derivative
Crystal parameters
Space group	P6522	P6522
Cell dimensions a, c (Å)	130.79, 147.74	131.58, 148.60	131.41, 148.31	131.59, 148.61	131.72, 148.57
Data collection
Wavelength (Å)	0.9000	0.9950	0.9793	0.9789	0.9640
Resolution range (Å)a	20–2.5	20–2.7	20–2.7	20–2.7	20–2.7
Total reflections	156019	395194	388809	389697	390047
Unique reflectionsa	26252 (1277)	21282 (1037)	21353 (1055)	21258 (1037)	21387 (1058)
Rmergeab	0.081 (0.487)	0.070 (0.439)	0.078 (0.436)	0.083 (0.417)	0.091 (0.590)
Average I/σ(I)ac	11.6 (4.4)	13.6 (6.2)	13.1 (6.0)	13.5 (6.3)	12.1 (5.7)
Completenessa	0.999 (1.000)	0.999 (1.000)	0.999 (1.000)	0.999 (1.000)	0.999 (1.000)
Redundancya	5.9 (6.0)	18.6 (19.0)	18.2 (17.9)	18.3 (18.8)	18.2 (17.9)
Refinement		MAD phasing
Resolution range (Å)	20–2.5	No. of selenium sites		8
R-factor / free R-factorde	0.194/0.230	Mean figure of merit
Atoms in an asymmetric unit		acentric		0.564
Protein	3675	centric		0.343
Ligand (ADP, P-analog, 2 Mg)	51
Water	147
Deviations from ideal geometry
Bonds distances (Å)	0.009
Angles (°)	1.295
Mean isotropic equivalent B-factors
Main-chain (Å2)	22.3
Side-chain (Å2)	23.0
Ligand (Å2)	22.5
Water (Å2)	22.7
Ramachandran plotf
Favored	0.959
Allowed	0.041

^aValues in parentheses are for highest resolution shells.

^bR_merge = Σ_hklΣ_i(|I_i (hkl)- <I(hkl)>|)/ Σ_hklΣ_iI_i(hkl).

^cSignal-to-noise ratio of intensities.

^dR = Σ(|F_o − F_c|)/ΣF_o.

^eFive percent of reflections were randomly chosen for calculation of free R value.

^fValues from Rampage.³⁷