2IOO
Crystal structure of the mouse p53 core domain
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU |
| Temperature [K] | 92.15 |
| Detector technology | IMAGE PLATE |
| Detector | RIGAKU RAXIS IV |
| Wavelength(s) | 1.5418 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 91.568, 44.709, 62.607 |
| Unit cell angles | 90.00, 125.61, 90.00 |
Refinement procedure
| Resolution | 50.000 - 2.020 |
| Rwork | 0.210 |
| R-free | 0.22500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | Mouse p53 core domain |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.330 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 |
| High resolution limit [Å] | 2.020 | 2.020 |
| Rmerge | 0.044 | 0.198 |
| Number of reflections | 13086 | |
| <I/σ(I)> | 5.82 | 5.82 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 293 | 100mM Hepes, 16-18% PEG 2K MME, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |






