Table 1.
Selected X-ray intensity data collection, structure solution and refinement statistics
| MepR-DNA | MepR-DNA | MepR-DNA (SeMet) | |
|---|---|---|---|
| PDB accession code | 4LLN | 4LLL | |
| Data collection | |||
| Space group | P1 | P31 | P31 |
| Cell dimensions (Å, °) | 76.3 76.2 109.4 | 130.2 130.2 124.7 | 128.9 128.9 125.7 |
| 90.6 104.7 106.2 | 90.0 90.0 120.0 | 90.0 90.0 120.0 | |
| Wavelength (Å) | 1 | 1 | 0.979 |
| Resolution (Å) | 50-2.84 (2.90-2.84)a | 50-3.0 (3.05-3.00) | 50-3.65 (3.71-3.65) |
| Rmerge (%)b | 9.6 (69.2) | 8.1 (>100) | 10.8 (67.8) |
| I/σI | 31.7 (2.0) | 42.9 (2.0) | 33.2 (3.6) |
| Completeness (%) | 91.0 (65.4)c | 100 (100) | 100 (99.9) |
| Multiplicity | 7.3 (6.2) | 11.5 (11.1) | 11.9 (10.6) |
| SAD phasing | |||
| Resolution (Å) | 50-3.65 | ||
| Selenium sites | 40 | ||
| Figure of meritd | 0.58 | ||
| Refinement | |||
| Resolution (Å) | 44.84-2.84 | 42.61-3.04 | |
| Reflections | 47 769 | 45 454 | |
| Rwork/Rfree (%)e | 20.6/24.1 | 19.4/23.4 | |
| Protein atoms | 6352 | 8103 | |
| DNA atoms | 2934 | 2934 | |
| Solvent atoms | 0 | 0 | |
| Average B (Å2): protein/DNA | 74.2/80.0 | 77.2/71.4 | |
| RMSD bond lengths (Å) | 0.003 | 0.009 | |
| RMSD bond angles (°) | 0.915 | 1.533 |
aValues for the highest resolution shell are shown in parentheses.
bRmerge = ∑∑|Ihkl − Ihkl(j)| / ∑Ihkl, where Ihkl(j) is observed intensity and Ihkl is the final average value of intensity.
c80–100% completeness is observed for all resolution shells 3.0 Å and above.
dFigure of merit = <|∑P(α)eiα / ∑P(α)|>, where α is the phase and P(α) is the phase probability distribution.
eRwork = ∑||Fobs| − |Fcalc|| / ∑|Fobs| and Rfree = ∑||Fobs| − |Fcalc|| / ∑|Fobs|, where these reflections belong to a test set of 10% randomly selected data.