Table 1.
Summary of crystallographic analysis
| MAD data collection (53BP1–p53 complex) | MAD phasing statistics (15–2.7Å) | |||||||
|---|---|---|---|---|---|---|---|---|
| Wavelength (Å)
|
Resolution (Å)
|
Measured reflections
|
Unique reflections
|
Coverage (%)
|
Rsym (%)
|
Phasing power
|
Rcullis
|
Rcullis (ano)
|
| λ1 (1.2832) | 2.5 (2.6–2.5) | 169611 | 29872 | 89.4 (56.5) | 5.1 (17.8) | — | — | 0.84 |
| λ2 (1.2817) | 2.5 (2.6–2.5) | 170142 | 30000 | 89.4 (56.4) | 5.3 (18.6) | 0.71 | 0.88 | 0.79 |
| λ3 (1.2622) | 2.5 (2.6–2.5) | 172211 | 29847 | 89.5 (55.9) | 5.3 (21.7) | 0.88 | 0.84 | 0.83 |
| Refinement statistics | RMSD
|
|||||||
| Resolution range (Å) | Reflections (|F| > 0σ) | Atoms (total, water) | R-factor (%) | R-free (%) | bonds (Å) | angles (°) | B factor (Å2) | |
| 15–2.5 (2.6–2.5) | 28192 | 6988, 216 | 21.6 (32.1) | 25.6 (39.5) | 0.014 | 1.73 | 2.2 | |
| MIR data collection (rat Brca1) | MIR phasing statistics (15–3.4Å) | |||||||
| Crystal | Resolution (Å) | Measured reflections | Unique reflections | Coverage (%) | Rsym (%) | Phasing power | Rcullis | |
| Native | 2.1 (2.18–2.10) | 55198 | 17223 | 97.0 (97.9) | 8.2 (45.7) | — | — | |
| Thimerosal | 3.7 (3.87–3.70) | 16590 | 3662 | 98.9 (98.5) | 14.8 (22.8) | 1.48 | 0.75 | |
| K2PtCl4 | 2.8 (2.90–2.80) | 24596 | 7387 | 99.1 (99.0) | 8.7 (32.3) | 0.93 | 0.85 | |
| Refinement statistics | RMSD | |||||||
| Resolution range (Å) | Reflections (|F| > 0σ) | Atoms (total, water) | R-factor (%) | R-free (%) | bonds (Å) | angles (°) | B factor (Å2) | |
| 15–2.3 (2.4–2.3) | 12529 | 1702, 177 | 20.3 (26.2) | 25.8 (34.1) | 0.011 | 1.61 | 4.5 | |
Coverage (%) indicates the percentage of total theoretically observable reflections measured. Rsym = ΣhΣi |Ih,i − Ih|/ΣhΣiIh,i, where Ih is the mean intensity of the i observations of reflection h. Phasing power = [FH(calc)2/(FPH(obs) − FPH(calc))2]1/2, where FPH(obs) and FPH(calc) are the observed and calculated derivative structure factors, respectively. Rcullis is the mean residual lack-of-closure error divided by the dispersive or anomalous difference. Figure of Merit (FOM) = <Σ P(α) exp(iα)/ΣP(α)>, where P(α) is the probability distribution for the phase α. R = Σ |Fobs − Fcalc|/ΣFobs, where Fobs = FP, and Fcalc is the calculated protein structure factor from the atomic model. R-free is the R factor calculated using 5% of the reflection data chosen randomly and omitted from the refinement process, and R-factor is calculated with the remaining data in the refinement. The root means square deviation (RMSD) values in bond lengths and angles are deviations from ideal values, and the RMSD values in B factors are calculated between covalently bonded atoms.