Table 2.

Data processing and refinement statistics for the PCV2 crystal structure^a

Statistic or parameterb	Value for statistic or parameter
	Useful data	Outer shell
Data collection statistics
Resolution range (Å)	40.0–2.35	2.43–2.35
Completeness (%)	68.7	44.8
No. of unique reflections	1,002,451	65,270
Rmerge (%)c	7.1	27.8
Avg I/σI	6.2	1.4
Redundancyd	1.9	1.3
Refinement statistics
Resolution range (Å)	40.0–2.35	2.46–2.35
Completeness (%)	68.7	44.9
No. of unique reflections	1,002,451	81,840
Rcryst (%)e	24.5	39.6
No. of atomsf (Ca atoms)	1,740 (194)
No. of water molecules and ions	131
Protein geometry and thermal parameters
RMSDb from ideality
Bond length (Å)	0.007
Angle (°)	1.4
Average temperature factor (Å2)
Protein	25.8
Water molecules and ions	38.6
Ramachandran plot (%)
Favored	89.2
Allowed	10.2
Outliers	0.6

^aValues given are for data with I/σ_I ≥ 0. The space group is P1 with unit cell dimensions a = 193.6 Å, b = 202.2 Å, c = 231.0 Å, α = 90.0°, β = 89.3°, and γ = 90.1°.

^bI/σ_I, measured intensity divided by measured error; RMSD, root mean square deviation.

^cR_merge = (Σ_hΣ_i (I_hi − <I_h>)/Σ_hΣ_i I_h) × 100 where <I_h> is the mean of the I_hi observations of reflection h.

^dRedundancy is the number of observations/number of unique reflections.

^eR_cryst = (Σ_h|F_o − F_c|/Σ_hF_o) where F_o and F_c are the observed and calculated structure factors, respectively.

^fNumber for all nonhydrogen atoms, including water molecules and ions.