Table 1.

Statistics for crystallographic structure determinations

Data set	1	2
Data collection site	SRS PX14.2	ESRF ID14-EH2
Wavelength, Å	0.979	0.933
Unit cell (a, b, c in Å)	151.9, 111.9, 82.5	149.8, 107.8, 82.2
Resolution range, Å	25.0–3.30	30.0–2.35
Observations	112,302	631,721
Unique reflections	21,667	56,142
Completeness, %	99.5	100
I/σI	5.2	16.0
Rmerge	0.239	0.128
Outer resolution shell
Resolution range, Å	3.42–3.30	2.43–2.35
Unique reflections	2,072	5,520
Completeness, %	97.9	100
I/σI	1.3	1.1
Refinement statistics:
Resolution range, Å		30.0–2.35
No. of reflections (working/test)		53236/2838
R factor (Rworking/Rfree)		0.189 (0.194/0.241)
No. of atoms (protein/water/others)		7,744/284/160
rms bond length deviation, Å		0.0081
rms bond angle deviation, °		1.39
Mean B factor, Å2		50/58/48/107
rms backbone B-factor deviation		4.5

^*R_merge = Σ|I − 〈I〉|/Σ〈I〉.

^† R factor = Σ|F_o − F_c|/ΣF_o.

^‡ Mean B factor for main-chain, side-chain, water, and other molecules (sulfate and glycerol), respectively.

^§ rms deviation between B-factors for bonded main-chain atoms.