TABLE 1.

X-ray crystallographic data and refinement statistics for the crystals of GRASP65 and GRASP55

	Crystals
	GRASP65	GRASP55
Data collection
Space group	P21212	P43212
Wavelength (Å)	0.9795	0.9793
Unit cell dimensions
a (Å)	44.99	83.08
b (Å)	104.29	83.08
c (Å)	37.93	145.15
α, β, γ	90°, 90°, 90°	90°, 90°, 90°
Molecules/ASUa	1	2
Resolution (Å)b	2.2 (2.28-2.20)	2.7 (2.82-2.70)
Completeness (%)b	99.3 (96.0)	98.2 (93.2)
Redundancyb	6.4 (5.6)	10.9 (10.1)
No. of total reflections	60,785	156976
No. of unique reflections	9540	14,443
I/σb	17.5 (2.4)	10.7 (1.6)
Rsymb,c	6.3 (27.4)	8.3 (56.5)
Refinement statistics
Resolution (Å)	2.2	2.7
No. of reflections	9498	14,320
Rwork/Rfree (%)d,e	20.33/26.46	20.24/28.99
No. of atoms
Protein	1549	3231
Ligand/ion	2	0
Water	139	91
B-factors (Å2)
Protein	32.37	68.34
Water	34.27	46.17
r.m.s.d.
Bond length (Å)	0.008	0.008
Bond angle	1.169°	1.112°
Ramachandran analysis
Most favored (%)	79.6	80.2
Additional allowed (%)	17.4	16.1
Generously allowed (%)	3.0	3.7
Disallowed (%)	0	0

^a ASU, asymmetric unit; r.m.s.d., root mean square deviation.

^b Values in parentheses are for the highest resolution shell.

^c R_sym = Σ|I − 〈I〉|/Σ〈I〉, where I is the observed intensity, and 〈I〉 is the average intensity of multiple observations of symmetry-related reflections.

^d R = Σ_hkl|F_obs| − |F_calc|/Σ_hkl|F_obs|.

^e R_free was calculated from 5% of the reflections excluded from refinement.