3D05
Human p53 core domain with hot spot mutation R249S (II)
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 | 2004-12-06 |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 0.9760 |
Spacegroup name | P 65 2 2 |
Unit cell lengths | 44.374, 44.374, 330.026 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 34.840 - 1.700 |
R-factor | 0.22053 |
Rwork | 0.218 |
R-free | 0.26383 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1tsr |
RMSD bond length | 0.012 |
RMSD bond angle | 1.341 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 35.000 | 1.740 |
High resolution limit [Å] | 1.700 | 1.700 |
Number of reflections | 22189 | |
<I/σ(I)> | 22.9 | 5.1 |
Completeness [%] | 96.6 | 84 |
Redundancy | 7.8 | 4.6 |
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 |