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. 2016 Jan 1;72(Pt 1):131–146. doi: 10.1107/S2059798315022111

Table 1. Data-collection, refinement and model statistics.

Values in parentheses are for the outer shell.

PDB entry 4wzj
Data collection
 Wavelength (Å) 0.9795
 Space group P31
 Unit-cell parameters (Å, °) a = b = 248.0, c = 251.9, α = β = 90.00, γ = 120.00
 Resolution (Å) 68.20–3.47 (3.66–3.47)
R merge (%) 20.9 (72.8)
 Unique reflections 220236
 Mean I/σ(I) 3.3 (1.1)
 CC1/2 0.991 (0.234)
 Completeness (%) 98.6 (97.8)
 Average multiplicity 2.0 (1.9)
Refinement
 Resolution (Å) 66.15–3.60 (3.69–3.60)
R work/R free 0.177/0.224 (0.260/0.270)
 No. of reflections (R work/R free) 158528/8251 (3086/152)
 Completeness (%) 83.1 (21.8)
 Twin operators and estimated twin fractions
   h, k, l 0.2177
  −k, −h, −l 0.2825
   k, h, −l 0.2833
  −h, −k, l 0.2165
Model
 No. of atoms
  Total 71485
  Protein 54046
  RNA 17436
  Water 3
 R.m.s. deviations from ideal geometry§
  Bond lengths (Å) 0.0105
  Bond angles (°) 1.399
B factors (Å2)
  Overall 124.4
  Protein 118.4
  RNA 162.8
  Water 42.7
 Ramachandran plot
  Favoured (%) 96.74
  Outliers (%) 0.13
MolProbity †† score [percentile] 1.78 [100th]
 All-atom clashscore [percentile] 11 [97th]
 Good rotamers (%) 98.95
 Good RNA backbone conformation (%) 98.16

CC1/2 = 0.516 at 3.88–3.66 Å.

Values after correction for diffraction aniso­tropy.

§

Using the REFMAC5 dictionary (Vagin et al., 2004).

Lovell et al. (2003).

††

Chen et al. (2010).