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 |