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. 2014 Apr 25;70(Pt 5):583–587. doi: 10.1107/S2053230X14007845

Table 1. Data-collection statistics.

Values in parentheses are for the highest of 20 resolution shells.

Diffraction data
 Space group P3221
 Unit-cell parameters (Å) a = b = 98.96, c = 199.26
 Resolution (Å) 50–2.35 (2.41–2.35)
 Mean I/σ(I) 13.8 (2.6)
R merge 0.069 (0.563)
R mean 0.079 (0.635)
 CC1/2 99.8 (81.9)
 Completeness (%) 99.8 (99.9)
 Multiplicity 4.6 (4.7)
 No. of unique reflections 47821 (3479)
 Wilson B factor (Å2) 40.4
Refinement
 No. of protein atoms 5859
 No. of waters 274
 No. of other atoms 50
R work 0.173 (0.261)
R free § 0.206 (0.325)
 R.m.s.d., bonds (Å) 0.012
 R.m.s.d., angles (°) 1.35
 Ramachandran, favoured 745 [97.9%]
 Ramachandran, outliers None
 Average B factor (Å2)
  Overall 55.8
  Protein 56.3
  Solvent 43.5
MolProbity clashscore 1.31 [100th percentile]
MolProbity score 0.88 [100th percentile]
 PDB entry 4ix8

R merge = Inline graphic Inline graphic.

R work = Inline graphic Inline graphic.

§

The free R factor was calculated with an equivalent equation to R work using 5% of the reflections that were omitted from the refinement.

Chen et al. (2010).