3D0A
Human p53 core domain with hot spot mutation R249S and second site suppressor mutation H168R in sequence-specific complex with DNA
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 | 2005-07-01 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.97565 |
| Spacegroup name | P 1 |
| Unit cell lengths | 54.299, 57.986, 78.926 |
| Unit cell angles | 83.05, 88.11, 74.08 |
Refinement procedure
| Resolution | 17.760 - 1.800 |
| R-factor | 0.18586 |
| Rwork | 0.183 |
| R-free | 0.24134 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2ac0 |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.586 |
| 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] | 17.760 | 1.830 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Number of reflections | 83720 | |
| <I/σ(I)> | 14.6 | 4.4 |
| Completeness [%] | 96.6 | 85.2 |
| Redundancy | 3.1 | 2.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.1 | 293 | 0.2 M ammonium formate, 20% PEG 3350, pH 6.1, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
Crystallization Reagents
| ID | crystal ID | solution ID | reagent name | concentration | details |
| 1 | 1 | 1 | ammonium formate | ||
| 2 | 1 | 1 | PEG 3350 | ||
| 3 | 1 | 1 | H2O | ||
| 4 | 1 | 2 | ammonium formate | ||
| 5 | 1 | 2 | PEG 3350 | ||
| 6 | 1 | 2 | H2O |
