5MCV
New Insights into the Role of DNA Shape on Its Recognition by p53 Proteins (complex p53DBD-LWC1)
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 | 2013-07-20 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.88560 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 138.078, 49.533, 68.047 |
| Unit cell angles | 90.00, 92.91, 90.00 |
Refinement procedure
| Resolution | 34.475 - 1.600 |
| R-factor | 0.1558 |
| Rwork | 0.154 |
| R-free | 0.18780 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | PDBID 1TSR |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.968 |
| 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] | 35.000 | 35.000 | 1.630 |
| High resolution limit [Å] | 1.600 | 4.340 | 1.600 |
| Rmerge | 0.073 | 0.045 | 0.394 |
| Rmeas | 0.080 | 0.049 | 0.448 |
| Rpim | 0.033 | 0.020 | 0.209 |
| Total number of observations | 346296 | ||
| Number of reflections | 60494 | ||
| <I/σ(I)> | 5.2 | ||
| Completeness [%] | 99.4 | 99.5 | 97.5 |
| Redundancy | 5.7 | 5.9 | 4.3 |
| CC(1/2) | 0.999 | 0.940 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 8.8 | 292 | 0.02 M Citric acid, 0.08 M BIS-TRIS propane, 16% w/v Polyethylene glycol 3,350 |
