3V3B
Structure of the Stapled p53 Peptide Bound to Mdm2
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X10SA |
| Synchrotron site | SLS |
| Beamline | X10SA |
| Temperature [K] | 90 |
| Detector technology | PIXEL |
| Collection date | 2011-02-07 |
| Detector | PSI PILATUS 6M |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 45.400, 42.410, 50.500 |
| Unit cell angles | 90.00, 90.86, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.000 |
| R-factor | 0.16827 |
| Rwork | 0.166 |
| R-free | 0.21647 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.050 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0072) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 50.000 |
| High resolution limit [Å] | 2.000 |
| Number of reflections | 13254 |
| Completeness [%] | 99.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4.75 | 290 | 100 mM Na-acetate, 2.5M NaCl, pH 4.75, VAPOR DIFFUSION, SITTING DROP, temperature 290K |
