4IBY
Human p53 core domain with hot spot mutation R273H and second-site suppressor mutation S240R
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-3 |
| Synchrotron site | ESRF |
| Beamline | ID14-3 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-04-27 |
| Detector | ADSC QUANTUM 4r |
| Wavelength(s) | 0.9310 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 43.524, 69.212, 67.195 |
| Unit cell angles | 90.00, 96.61, 90.00 |
Refinement procedure
| Resolution | 21.779 - 1.450 |
| R-factor | 0.171 |
| Rwork | 0.169 |
| R-free | 0.20030 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1tsr |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.130 |
| 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] | 25.000 | 25.000 | 1.470 |
| High resolution limit [Å] | 1.450 | 3.930 | 1.450 |
| Rmerge | 0.077 | 0.038 | 0.537 |
| Number of reflections | 69956 | ||
| <I/σ(I)> | 8.8 | ||
| Completeness [%] | 99.7 | 99.3 | 100 |
| Redundancy | 4.2 | 4.2 | 4.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.1 | 293 | 20% PEG 3350, 0.2M Na2HPO4, pH 6.1, Vapor diffusion, hanging drop, temperature 293K |
