TABLE 1.

Crystallographic statistics

Diffraction data	Crystal I (SeMet)	Crystal II (Native)
Data set
Unit cell a, b, c (Å)	63.67, 108.78, 111.89	63.70, 108.82, 111.99
Resolution range (Å)	30–2.2	2.28 – 2.2	30–2.25	2.33–2.25
Reflections
observed	431,614	40,762	288,667	19,524
unique	40,114	3941	37,455	3454
Completeness (%)	99.7	99.6	99.1	92.7
〈I〉/〈σ(I) 〉	43.1	7.2	30.6	4.0
Rsyma (%)	0.07	0.414	0.062	0.395
SIRAS analysis
Resolution range (Å)	30–2.2	2.28–2.2
Rderivb	0.062	0.155
Mean figure of meritc	0.35	0.20
Phasing power (centric)d	1.04	0.44
Phasing power (acentric)	1.23	0.52
Refinement
Resolution range (Å)	30–2.2	2.28–2.2
Rfreee	0.254	0.324
Rwork	0.216	0.274
RMSD bonds/anglesf	0.0059 Å/1.23°
Coordinate errorg	0.27 Å

^aR_sym = ∑|I − 〈I〉|/∑ I where I is the observed intensity and 〈I〉 is the statistically weighted absolute intensity of multiple measurements of symmetry related reflections.

^bR_deriv = ∑||F_PH| − | F_p||/∑|F_p|, where |F_PH| and |F_p| are the heavy-atom derivative and protein structure factor amplitudes, respectively.

^cMean figure of merit = 〈∑ P(α)e^iα/∑P(α) >, where α is the phase and P(α) is the phase-probability distribution.

^dPhasing power = 〈|F_H|〉/〈||F_p + F_H| − |F_PH||〉, where |F_H| is the heavy atom structure factor amplitude; reported for centric and acentric reflections.

^eThe free-R factor was calculated with a randomly selected 10% of the reflections.

^fRoot mean square deviations (RMSD) from ideal bond lengths and angles.

^gCross-validated σA coordinate error.