Table 1. Crystallographic data collection and refinement statistics.
| Data Collection Statistics | |
| Wavelength (nm) | 0.9793 |
| Spacegroup | I422 |
| Unit Cell Parameters (a, b, c)(Å) | 129.5, 129.5, 152.6 |
| (α,β,γ)(°) | 90, 90, 90 |
| # Complexes/Asymmetric Unit | 1 |
| Unique Reflections | 22435 |
| Resolution Range (Å) | 40.00 – 3.1 (3.15 – 3.1) |
| Mean Redundancy | 5.7 (5.8) |
| Overall Completeness (%) | 99.7 (100.0) |
| Rmerge (%)(a) | 6.9 (54.3) |
| Mean I/σ | 29.0 (2.98) |
| # Se Atoms Found | 8 |
| FOM initial | 0.41 |
| FOM after density modification | 0.65 |
| Model Refinement Statistics | |
| Rwork (%) | 26.1 |
| Rfree (%)(b) | 29.5 |
| # Protein Atoms | 1522 |
| # DNA Atoms | 731 |
| # Water Molecules | 7 |
| RMSD Bond Angles (°) | 0.006 |
| RMSD Bond Lengths (Å) | 1.180 |
| Ramachandran Statisticsc | |
| Most Favored Regions | 153 (89.0%) |
| Additionally Allowed Regions | 19 (11.0%) |
| Generously Allowed Regions | 0 (0.0%) |
| Disallowed Regions | 0 (0.0%) |
a
Rmerge = (Σ|I−<I>|)/ΣI, where I is the observed intensity and <I> is the average intensity.
b
Rfactor = Σ∥Fo|−|Fc∥/Σ|Fo|. Rfree is calculated with the same equation, but with 5% of reflections not used in the refinement.
c
Ramachandran statistics are given as the number of amino acids that lie within each region, and the percentage is given in parenthesis.
Values in parenthesis are for the outermost resolution shell (3.15 Å – 3.1 Å).