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. 2011 Feb;278(3):541–549. doi: 10.1111/j.1742-4658.2010.07976.x

Table 2.

X-ray data collection and refinement statistics. Rsymm = Σh Σi |I(h) − Ii(h)|/Σh ΣiIi(h), where Ii(h) and I(h) are the ith and the mean measurements of the intensity of reflection h, respectively. Rcryst = Σh |FoFc|/ΣhFo, where Fo and Fc are the observed and calculated structure factor amplitudes of reflection h, respectively. Rfree is equal to Rcryst for a randomly selected 5.0% subset of reflections not used in the refinement

RNase A·N-acylsulfonamide 7 RNase A·N-acylsulfonamide 6
Space group C2 C2
Cell dimensions a = 101.0 Å a = 101.0 Å
b = 33.1 Å b = 33.2 Å
c = 72.6 Å c = 72.8 Å
α = γ = 90° α = γ = 90°
β = 90.4° β = 90.9°
Resolution range (Å) 50–1.72 50–1.72
Rsymm (outer shell) 0.060 (0.171) 0.062 (0.192)
I/σI (outer shell) 17.5 (6.0) 17.2 (5.7)
Completeness (outer shell) (%) 98.5 (94.5) 98.0 (92.7)
Total no. of reflections 174 818 186 775
Unique no. of reflections 26 158 26 200
Redundancy (outer shell) 3.0 (2.8) 3.1 (2.9)
Wilson B-factor (Å2) 17.8 18.1
Rcryst/Rfree 0.212/0.246 0.214/0.244
Average B-factor (Å2)
 Overall 18.1 18.3
 Protein (chain A, B) 16.2, 16.5 16.4, 16.3
 Ligand 21.8, 56.0 34.2, 43.2
 Solvent 26.5 25.6
rmsd
 Bond length (Å) 0.007 0.007
 Bond angle (°) 1.439 1.113
PDB codes 2xog 2xoi