Table 1.

Diffraction data and refinement statistics

	Crystal form 1	Crystal form 2
Resolution, Å	2.4	2.3
Measurements, n	78,773	46,925
Unique reflections	26,594	14,542
Data completeness	30–2.4 Å 91.2%	30–2.3 Å 96.2%
	2.53–2.4 Å 58.4%	2.4–2.3 Å 95.2%
Rsym on intensity*, %	5.7	8.5
Reflections used in refinement	24,386	14,081
R value†	8.0–2.4 Å 20.6%	8.0–2.3 Å 19.6%
R-free‡, %	29.4	28.7
rms deviation from ideal bond length, Å	0.008	0.007
rms deviation from ideal bond angle, °	1.31	1.24
B value for nonhydrogen protein atoms, Å2	24.1	15.6
rms deviation in B value of bonded atoms, Å2	1.74	1.64
Nonhydrogen atoms, n	5,433	2,790
Water molecules, n	302	211

^*R_sym = Σ|I(h) − 〈I(h)〉|/Σ I(h). 

^†R = Σ|F_o − F_c|/ΣF_o with F/Σ F > 2. 

^‡R-free, R value for 10% of the data, which were not included during crystallographic refinement.