Table I.

X-Ray Data Reduction and Crystallographic Refinement Statistics

(A) X-ray data reduction statistics
Space group	P422
Unit cell parameters (a = b, c)	105.45 Å, 330 Å
Wavelength	0.99999 Å
Resolution (last shell)	26.36–2.64 Å (2.78–2.64 Å)
R-mergea (last shell)	0.063 (0.377)
Total no. of observations	376,916 (12,653)
Total no. of unique reflections	52,570 (6182)
Average I/σ(I) (last shell)	19.9 (1.9)
Completeness (last shell)	0.952 (0.797)
Redundancy (last shell)	7.2 (2)

(B) Crystallographic refinement statistics
Space group	P41212
Unit cell parameters (a = b, c)	105.45 Å, 330 Å
Low (high) resolution limit	38.65–2.64 Å (2.71–2.64 Å)
No. of reflections, working set (last shell)	49,850 (2626)
No. of reflections, test set (last shell)	2666 (128)
R-factorb (last shell)	0.2003 (0.2340)
R-freec (last shell)	0.2294 (0.2703)
No. of residues	1023
No. of protein atoms	8540
No. of solvent atoms	537
Average B-factor (protein)	65.8 Å2
Average B-factor (solvent)	54.8 Å2
Overall anisotropy B11, B22, B33	0.61620 Å2, 0.61620 Å2, 1.23240 Å2
R.m.s.d. from ideal values
Bond length	0.008 Å
Bond angle	0.87°

^aR-merge = .

^bR-factor = , where <|F_calc|> denotes the expectation of |F_calc(hkl)| used in defining the likelihood refinement target.

^cThe free R-factor is a cross-validation residual calculated by using about 5% reflections, which were randomly chosen and excluded from the refinement.