3DAC
Structure of the human Mdmx protein bound to the p53 tumor suppressor transactivation domain
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X10SA |
| Synchrotron site | SLS |
| Beamline | X10SA |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-04-08 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.00 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 66.430, 30.810, 70.090 |
| Unit cell angles | 90.00, 107.43, 90.00 |
Refinement procedure
| Resolution | 24.490 - 1.800 |
| R-factor | 0.2071 |
| Rwork | 0.205 |
| R-free | 0.24292 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ycr |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.236 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.000 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.069 | 0.223 |
| Number of reflections | 24703 | |
| <I/σ(I)> | 15.9 | 6.9 |
| Completeness [%] | 94.5 | 85.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 300 | 30% PEG300, 0.1M MES, pH6.5, VAPOR DIFFUSION, SITTING DROP |
