4IBZ
Human p53 core domain with hot spot mutation R273C and second-site suppressor mutation T284R
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-07-05 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.97590 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 68.742, 70.413, 84.585 |
| Unit cell angles | 90.00, 89.92, 90.00 |
Refinement procedure
| Resolution | 26.692 - 1.920 |
| R-factor | 0.1807 |
| Rwork | 0.179 |
| R-free | 0.23290 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1aco chain A |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.069 |
| 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] | 27.000 | 27.000 | 1.950 |
| High resolution limit [Å] | 1.920 | 5.200 | 1.920 |
| Rmerge | 0.081 | 0.048 | 0.356 |
| Number of reflections | 60012 | ||
| <I/σ(I)> | 9.6 | ||
| Completeness [%] | 97.8 | 98.5 | 81.2 |
| Redundancy | 3.7 | 3.6 | 2.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.1 | 293 | 12% PEG 3350, 0.12M NH4-Acetate, pH 6.1, Vapor diffusion, hanging drop, temperature 293K |
