4UMN
Structure of a stapled peptide antagonist bound to Nutlin-resistant Mdm2.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSRRC |
| Synchrotron site | NSRRC |
| Temperature [K] | 100 |
| Collection date | 2014-04-07 |
| Spacegroup name | P 2 21 21 |
| Unit cell lengths | 39.076, 65.674, 105.683 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 105.680 - 1.990 |
| R-factor | 0.2023 |
| Rwork | 0.200 |
| R-free | 0.23683 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2axi |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.260 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0069) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.020 |
| High resolution limit [Å] | 1.970 | 1.970 |
| Rmerge | 0.050 | 0.340 |
| Number of reflections | 19576 | |
| <I/σ(I)> | 34.74 | 4.87 |
| Completeness [%] | 99.3 | 95.3 |
| Redundancy | 6.4 | 5.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.4 | 289 | 0.04 M CITRIC ACID, 0.06 M BIS-TRIS PROPANE PH 6.4, AND 20% PEG 3350 |
