6FJ5
New Insights into the Role of DNA Shape on Its Recognition by p53 Proteins (complex p53DBD-AGG-HG)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2013-07-21 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.88560 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 68.517, 98.024, 73.171 |
| Unit cell angles | 90.00, 93.39, 90.00 |
Refinement procedure
| Resolution | 49.012 - 2.051 |
| R-factor | 0.2002 |
| Rwork | 0.199 |
| R-free | 0.24380 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1tsr |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.028 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER (2.5.7) |
| Refinement software | PHENIX |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.090 |
| High resolution limit [Å] | 2.050 | 5.560 | 2.050 |
| Rmerge | 0.186 | 0.108 | 0.475 |
| Number of reflections | 59807 | ||
| <I/σ(I)> | 3.1 | ||
| Completeness [%] | 99.0 | 98.3 | 99.3 |
| Redundancy | 4.8 | 4.6 | 4.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 7 | 292 | 0.1 M Sodium formate pH 7.0, 12% w/v Polyethylene glycol 3,350 |
