2IOI
Crystal structure of the mouse p53 core domain at 1.55 A
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-BM |
| Synchrotron site | APS |
| Beamline | 19-BM |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 92.316, 44.688, 63.051 |
| Unit cell angles | 90.00, 126.25, 90.00 |
Refinement procedure
| Resolution | 30.000 - 1.550 |
| Rwork | 0.184 |
| R-free | 0.22800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.010 |
| RMSD bond angle | 2.200 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | AMoRE |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 30.000 |
| High resolution limit [Å] | 1.550 | 1.550 |
| Rmerge | 0.040 | 0.128 |
| Number of reflections | 30053 | |
| <I/σ(I)> | 31.5 | 11.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 293 | 100mM Tris, 16-18% PEG 2K MME, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
