Table 1. X-ray structure determination detail.
|
Data set |
E1 | E2 | E3 | Refinement |
|---|---|---|---|---|
| Space group | P43212 | P43212 | P43212 | P43212 |
| Wavelength (Å) | 0.97930 | 0.97916 | 0.96802 | 0.97918 |
| Unit cell parameters | ||||
| a = b, c (Å) | 106.91, 424.61 | 106.98, 424.24 | 106.83, 423.30 | 106.99, 423.36 |
| α = β = γ (°) | 90, 90, 90 | 90, 90, 90 | 90, 90, 90 | 90, 90, 90 |
| Resolution range (Å) | 30.0–3.2 | 30.0–3.2 | 30.0–3.2 | 30.0–3.1 |
| No. of unique reflections | 77309 | 77464 | 77076 | 45362a |
| Redundancy | 7.08 | 7.13 | 7.19 | 14.52 |
| I/σI (3.29–3.2 Å) | 12.16 (1.28) | 12.45 (1.54) | 12.26 (1.93) | 13.3 (1.95) |
| BWilson (Å2) | 100.7 | 93.88 | 90.13 | 104.36 |
| Completeness (%) | 99.8 | 99.8 | 99.8 | 99.8 |
| Rmerge (%)b | 18.2 | 18.0 | 14.7 | 11.4 |
| CC1/2 (last resolution shell) | 49.2 | 60.8 | 77.0 | 81.9 |
| Phasing power (iso/ano) | 0.0/1.045 | 0.214/0.995 | 0.877/0.812 | |
| Figure of merit at 3.2 Å | 0.38 | |||
| Structure Refinement | ||||
| Resolution (Å) | 3.1 | |||
| Rwork/Rfree c | 0.198/0.256 | |||
| RMSD | ||||
| Bond lengths (Å) | 0.01 | |||
| Bond angles (°) | 1.17 | |||
| Average B factor (Å2) | 142.33 | |||
| No. atoms | ||||
| Protein | 11442 | |||
| DNA | 846 | |||
| Ligands (Ca2+) | 6 | |||
| Waters | 36 | |||
| No. of reflections | 45362 | |||
| Ramachandran plot (%) | ||||
| Favored | 86.6 | |||
| Allowed | 13.1 | |||
| Outliers | 0.2 | |||
Numbers in parentheses represent the value for the highest-resolution shell. RMSD, root-mean-square deviation.
a Friedel's law true.
b Rmerge = Σ|Ii − <I>|/ΣIi, where Ii is the intensity of measured reflection and <I> is the mean intensity of all symmetry-related reflections.
c Rfree = ΣT||Fcalc| – |Fobs||/ΣFobs, where T is a test dataset of about 5% of the total unique reflections randomly chosen and set aside prior to refinement.