Table 1.
Space group | P1 | Unit cell | a = b = 249.7 Å, c = 644.8 Å; α = 90.0°, β = 101.2°, γ = 120.0° |
Data processing (three-fold-expanded in pseudo-R3) | Noncrystallographic averaging | ||
Observations | 747,988 | Redundancy | 180-fold |
Unique reflections | 495,356 | Correlation coefficients | |
Resolution | 100–3 Å (shell at 3.5 Å) | cc(2Fo − F〈map〉, φ〈map〉) | 0.78 |
Completeness | 56% (43%) (80% to 3.5 Å) | cc(Fo, F〈map〉) | 0.65 |
Rmerge | 0.156 (0.309) | R(Fo, F〈map〉) | 0.32 |
Model | |||
Amino acids | 180 × 519 | R/Rfree | 0.338/0.342 |
Missing | 1–14 (VP3) | rms deviations from ideal bond lengths/angles | 0.02 Å/2.2° |
Rmerge = ∑h∑i[Ih,i − 〈Ih〉]/∑h〈Ih〉, where Ih,i is the ith observation of a symmetry equivalent of reflection h.
F〈map〉, φ〈map〉 are Fourier terms of the back-transformed final averaged map.
Correlation between the densities of all noncrystallographic symmetry equivalent points.
Rfree is not unbiased. Test-set reflections are correlated to working-set reflections mapped to the neighborhood with noncrystallographic symmetry. However, with the high ratio of data to parameters, over-fitting will be negligible.