5MCT
New Insights into the Role of DNA Shape on Its Recognition by p53 Proteins (complex p53DBD-LHG1)
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 | 2014-04-28 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.976250 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 137.486, 49.460, 68.503 |
| Unit cell angles | 90.00, 93.63, 90.00 |
Refinement procedure
| Resolution | 46.529 - 1.446 |
| R-factor | 0.1466 |
| Rwork | 0.144 |
| R-free | 0.18900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | PDBID 1TSR |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.876 |
| 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 | 1.480 |
| High resolution limit [Å] | 1.450 | 3.940 | 1.450 |
| Rmerge | 0.090 | 0.057 | 0.419 |
| Rmeas | 0.098 | 0.062 | 0.462 |
| Rpim | 0.036 | 0.023 | 0.188 |
| Total number of observations | 510649 | ||
| Number of reflections | 80131 | ||
| <I/σ(I)> | 5.9 | ||
| Completeness [%] | 97.5 | 99.8 | 89.3 |
| Redundancy | 6.4 | 6.9 | 4.8 |
| CC(1/2) | 0.998 | 0.956 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 7 | 292 | 0.1 M Ammonium citrate, 12% w/v Polyethylene glycol 3,350 |
