Table 1.

Data Collection, Phasing, and Refinement Statistics

Data Collection
space group	I422
unit cell	a = b = 102.478 Å, c = 65.281 Å
wavelength (Å)	0.9685
resolution (Å)	2.1 (2.18–2.10)a
Rsym (%)b	5.6 (19.0)a
〈I/σI〉c	>20 (20)a
completeness (%)d	99.9 (100)a
redundancy	14.3 (14.7)a
Refinement
resolution (Å)	2.1
R-factor (%)e	21.7
Rfree (%)f	22.4
no. of protein atoms	784
no. of water molecules	60
no. of unique reflections	10431
rmsdg
bonds (Å)	0.005
angles (deg)	1.1

^aStatistics for the highest-resolution bin of reflections in parentheses.

^bR_sym = Σ_hΣ_j|I_hj − 〈I_h〉|/Σ_hΣ_jI_hj, where I_hj is the intensity of observation j of reflection h and 〈I_h〉 is the mean intensity for multiply recorded reflections.

^cIntensity of the signal-to-noise ratio.

^dCompleteness of the unique diffraction data.

^eR-factor = Σ_h‖F_o| − |F_c‖/Σ_h|F_o|, where F_o and F_c are the observed and calculated structure factor amplitudes, respectively, for reflection h.

^fR_free is calculated against a 10% random sampling of the reflections that were removed before structure refinement.

^gRoot-mean-square deviation.