Table 1.
Crystallographic data collection and refinement
| A. Data collection and phasing statistics | |
| Total no. of reflections | 131 820 |
| Resolution range (Å) | 20–2.3 |
| No. of unique reflections | 32 438 |
| Rsym (last shell) | 0.042 (0.108) |
| Completeness (%) (last shell) | 89 (84) |
| I/σ(I) | 43.2 (20.8) |
| Redundancy (last shell) | 4.1 (4.0) |
| B. Refinement statistics | |
| Resolution range (Å) | 20–2.3 |
| No. of reflections used in refinement | 30 786 |
| Rcryst/Rfree | 0.16/0.23 |
| No atoms | |
| Protein | 6007 |
| DNA | 972 |
| Water | 710 |
| Average B factors (Å2) | 14.2 |
| R.m.s. deviations | |
| Bonds (Å) | 0.017 |
| Angles (deg.) | 1.9 |
aRsym = ∑|In – < In>/∑In over all h, where In is the intensity of the reflection h.
bRcryst/Rfree = ∑||Fo| – |Fc|| / ∑|Fo|.
Rfree was calculated with 5% of data excluded from refinement.