Table 1.

Crystallographic statistics of the LC/X X-ray crystal structures.

	LC/X	Apo-LC/X
PDB code	6F47	6F4E
Synchrotron source, λ	Diamond I02, 0.979 Å	SLS PXI, 1.00 Å
Resolution (Å)	1.35 (1.37–1.35)	2.4 (2.49–2.40)
Space group	P212121	P22121
Cell dimensions and angles	a = 58.3, b = 86.7, c = 93.1 Å; α = β = γ = 90°	a = 52.3, b = 94.5, c = 113.0 Å; α = β = γ = 90°
Total/Unique reflections	592,965 98,954	176,299 21,016
Completeness (%)a	94.9 (64.8)	93.4 (88.9)
R merge a,b	0.083 (0.98)	0.123 (0.97)
R pim a,c	0.053 (0.74)	0.062 (0.52)
I/σ(I)a	9.2 (1.0)	8.9 (2.1)
CC1/2d	0.99 (0.42)	0.99 (0.69)
Multiplicity	6.0 (3.9)	8.4 (7.8)
Rcryste (%)	14.3	21.5
Rfreef (%)	17.6	26.0
Rmsd in bond lengths (Å)	0.009	0.009
Rmsd in bond angles (°)	1.34	1.31
B- factor statistics (Å 2 )
Protein all atoms	20.3	53.6
Protein main chain atoms	18.4	51.4
Protein side chain atoms	22.2	55.7
Solvent atoms	36.0	46.8
Zn2+ ion	18.2 (0.33 occupancy)	n/a
Ramachandran statistics (Molprobity)
Favored	97.7%	97.1%
Outliers	0.0%	0.0%

^aValues in parentheses refer to the highest resolution shell.

^bR_merge = ΣΣ_i|I_h − I_hi|/ΣΣ_iI_h, where I_h is the mean intensity for reflection h.

^cR_pim = Σ_h (1/n_h − 1) Σ_l |I_hl − (I_h)|/Σ_hΣ_l(I_h).

^dCorrelation coefficient between random half datasets.

^eR_cryst = Σ‖F_o| − |F_c‖/Σ|F_o|, where F_o and F_c are measured and calculated structure factors, respectively.

^fR_free = Σ‖F_o| − |F_c|/Σ|F_o|, calculated from 5% of the reflections selected randomly and omitted during refinement.