3D08
Human p53 core domain with hot spot mutation R249S and second-site suppressor mutation H168R
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID29 |
Synchrotron site | ESRF |
Beamline | ID29 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2005-03-16 |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 0.97564 |
Spacegroup name | P 65 2 2 |
Unit cell lengths | 46.287, 46.287, 327.445 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 34.200 - 1.400 |
R-factor | 0.1991 |
Rwork | 0.198 |
R-free | 0.21189 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1tsr |
RMSD bond length | 0.008 |
RMSD bond angle | 1.168 |
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] | 34.200 | 1.420 |
High resolution limit [Å] | 1.400 | 1.400 |
Number of reflections | 41783 | |
<I/σ(I)> | 30.4 | 8.9 |
Completeness [%] | 97.5 | 83.9 |
Redundancy | 11.8 | 8.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.1 | 293 | 0.2M Sodium acetate, 20% PEG3350, pH 6.1, VAPOR DIFFUSION, HANGING DROP, temperature 293K |