4IBW
Human p53 core domain with hot spot mutation R273H and second-site suppressor mutation T284R in sequence-specific complex with DNA
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-2 |
| Synchrotron site | ESRF |
| Beamline | ID14-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-02-25 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.9330 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 137.562, 49.923, 34.239 |
| Unit cell angles | 90.00, 93.68, 90.00 |
Refinement procedure
| Resolution | 34.320 - 1.791 |
| R-factor | 0.1441 |
| Rwork | 0.142 |
| R-free | 0.18760 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2ac0 chain A |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.146 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | PHENIX (1.8.1_1168) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 40.000 | 40.000 | 1.820 |
| High resolution limit [Å] | 1.790 | 4.860 | 1.790 |
| Rmerge | 0.117 | 0.047 | 0.536 |
| Number of reflections | 21929 | ||
| <I/σ(I)> | 6.7 | ||
| Completeness [%] | 100.0 | 100 | 100 |
| Redundancy | 7.4 | 6.9 | 7.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.1 | 293 | 1:2.4 PROTEIN/DNA RATIO, 14% PEG 3350, 0.14M NH4F, pH 6.1, Vapor diffusion, hanging drop, temperature 293K |
