TABLE 1.

Crystallographic data and refinement statistics

mol, molecules; r.m.s.d., root mean square deviation; ESRF, European Synchrotron Radiation Facility.

	CdFicSE/AA	CdFicSE/AA-ATP	CdFic
Data collection
Radiation source	MAX-II I911-2	ESRF ID29	ESRF ID23
Wavelength (Å)	1.038	0.900	0.873
Data processing
Space group	P212121	C2	C2221
Protein mol/AU	2	4	4
Cell dimensions	a = 52.4 Å, b = 67.3 Å, c = 139.6 Å, α = β = γ = 90°	a = 158.1 Å, b = 60.1 Å, c = 124.8 Å, α = γ = 90°, β = 118.6°	a = 57.4, b = 157.4, c = 262.7, α = β = γ = 90°
Resolution (Å)	20.0–1.8 (1.9–1.8)a	20.0–2.5 (2.6–2.5)	20.0–3.1 (3.2–3.1)
Completeness (%)	98.6 (97.2)	99.7 (100)	99.9 (99.9)
CC1/2b	99.9 (77.9)	99.9 (57.9)	99.6 (82.1)
Mean I/σ	19.0 (2.3)	16.7 (1.3)	9.7 (1.7)
Multiplicity	6.6 (6.5)	6.9 (7.2)	8.0 (8.4)
Rmeasc	7.7 (95.7)	8.2 (155.2)	17.3 (114.0)
Refinement
Resolution (Å)	19.1–1.8	19.9–2.5	19.9–3.1
Reflectionswork	45,953	35,839	20,454
Reflectionstest	1,378	1,076	1,026
Rworkd/Rfreee	18.4/21.8	20.48/23.3	23.3/28.6
Protein atoms	3,470	6,743	6,561
Water atoms	216	14
Glycerol/PO4/Hepes atoms	50
ATP/Mg2+ atoms		32
Overall B-factor (Å2)	26.3	67.3	51.9
r.m.s.d. bond lengths (Å)	0.008	0.010	0.003
r.m.s.d. bond angles (°)	0.999	0.921	0.779
Ramachandran statistics (%)
Favored	99.0	98.4	98.3
Allowed	1.0	1.5	1.7
Outliers	0	0.1	0
Protein Data Bank code	4X2C	4X2D	4X2E

^a Values in parenthesis are for the highest resolution shell.

^b Percentage of correlation between intensities from random half-data sets (65).

^c R_meas = Σ_hkl(N(hkl)/[N(hkl) − 1])^1/2Σ|I_i(hkl) − 〈/I(hkl)〉|Σ_hklΣI_i(hkl). Redundancy-independent R factor calculated on intensities (66).

^d R = Σ‖F_obs| − |F_calc‖Σ|F_obs| where |F_obs| and |F_calc| are observed and calculated structure factor amplitudes, respectively.

^e The R_free value was calculated with a random 3 or 5% subset of all reflections excluded from refinement.