Table 3.

X-ray diffraction data collection and refinement statistics.

	SARS-CoV PLpro-βME complex	SARS-CoV PLpro-glycerol complex
Data collection
Space group	C2	C2
Cell dimensions
a, b, c (Å)	151.4, 33.3, 90.7	151.2, 33.4, 90.9
α, β, γ (°)	90, 125, 90	90, 125, 90
Resolutiona (Å)	30–1.65 (1.71–1.65)	30–1.65 (1.71–1.65)
Rmergeb (%)	4.1 (34.7)	4.7 (45.6)
I/σI	29.0 (3.6)	26.3 (3.6)
Completeness (%)	99.7 (98.2)	95.5 (94.8)
Redundancy	3.6 (3.6)	3.5 (3.7)
Refinement
Number of reflections	42,759 (6082)	41,221 (5917)
R factorc (%)	14.7 (16.3)	16.2 (17.7)
Free R factord (%)	18.4 (20.1)	19.9 (21.7)
Number of atoms	2994	2899
Protein	2676	2659
Ligand/ion	16/6	18/6
Water	298	216
B-factors (Å2)
Protein	16.5	27.8
Ligand/ion	27.0/21.3	34.5/31.8
Water	28.2	34.8
rmsd
Bond length (Å)	0.007	0.008
Bond angles (°)	1.3	1.3
Ramachandran analysis (%)
Favored	92.3	93.0
Allowed	7.7	7.0

^aThe numbers in parentheses are for the highest-resolution shell.

^b$R_{merge}=\sum _h\sum _i|I_{hi}-〈I_h〉|/\sum _h\sum _i{I}_{hi}$, where $I_{hi}$ is the integrated intensity of a given reflection and $〈I_h〉$ is the mean intensity of multiple corresponding symmetry-related reflections.

^c$R=\sum _h|F_h^o-F_h^c|/\sum _h{F}_h^o$, where $F_h^o$ and $F_h^c$ are the observed and calculated structure factors, respectively.

^dFree R is R calculated using a random 5% of data excluded from the refinement.