3D09
Human p53 core domain with hot spot mutation R249S and second-site suppressor mutations H168R and T123A
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-1 |
| Synchrotron site | ESRF |
| Beamline | ID14-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-07-02 |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 0.93400 |
| Spacegroup name | P 65 2 2 |
| Unit cell lengths | 45.518, 45.518, 327.424 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 37.090 - 1.900 |
| R-factor | 0.20678 |
| Rwork | 0.204 |
| R-free | 0.26209 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1tsr |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.422 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP (- CCP4) |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 44.000 | 1.930 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Number of reflections | 17068 | |
| <I/σ(I)> | 33.5 | 4.5 |
| Completeness [%] | 98.8 | 90.4 |
| Redundancy | 9.9 | 5.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.1 | 293 | 0.2M Sodium Acetate, 20% PEG 3350, pH 6.1, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
