Table I. Data collection, structure determination and refinement statistics.

Data collection and MIR phasing statistics
Data set	Resolution (Å)	Observations/unique reflections	Completeness (last shell) %	Rmergea (last shell)
SeMet λ1	3.2	78580/60509	88.9 (84.1)	0.047 (0.15)
SeMet λ2	3.2	86114/63424	92.8 (85.4)	0.066 (0.25)
Native	2.6	259515/71198	99.3 (99.2)	0.084 (0.28)
Structure refinement statistics
Resolution (Å)	Protein atoms	Waters	Rcrystb	Rfreeb (% data used)	R.m.s.d. from idealityc
					Bonds	Angles	Dihedrals
25.0–2.6	9551	121	26.46	29.43 (3)	0.0072	1.3921	24.76

^aR_merge = Σ_hklΣ_i|I_i(hkl) – <I(hkl)>|/Σ_hklΣ_i I_i(hkl).

^bR_cryst and R_free = Σ|F_obs – F_calc|/ΣF_obs; R_free calculated with the percentage of the data shown in parentheses.

^cR.m.s.ds for bond angles and lengths in regard to Engh and Huber parameters.