5XXK
Structure-activity studies of Mdm2/Mdm4-binding stapled peptides comprising non-natural amino acids
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSRRC BEAMLINE BL13C1 |
| Synchrotron site | NSRRC |
| Beamline | BL13C1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-10-10 |
| Detector | RAYONIX MX300-HS |
| Wavelength(s) | 0.975 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 65.520, 106.410, 39.300 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 25.160 - 1.660 |
| R-factor | 0.18856 |
| Rwork | 0.187 |
| R-free | 0.20880 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4umn |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.452 |
| Data reduction software | xia2 |
| Data scaling software | xia2 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 25.160 | 1.700 |
| High resolution limit [Å] | 1.660 | 1.660 |
| Rmerge | 0.047 | 0.685 |
| Rpim | 0.022 | 0.323 |
| Number of reflections | 33120 | 2414 |
| <I/σ(I)> | 16.6 | 2.3 |
| Completeness [%] | 99.4 | 99 |
| Redundancy | 6.4 | 6.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.4 | 289 | 0.04M Citric acid, 0.06M Bis-Tris propane pH 6.4, 20% (v/v) PEG 3350 |
