5AFG
Structure of the Stapled Peptide Bound to Mdm2
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Temperature [K] | 100 |
| Collection date | 2014-11-13 |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 36.821, 36.821, 177.416 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 44.350 - 1.900 |
| R-factor | 0.1787 |
| Rwork | 0.176 |
| R-free | 0.22616 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4hg7 |
| RMSD bond length | 0.023 |
| RMSD bond angle | 1.947 |
| Data reduction software | PROTEUM2 |
| Data scaling software | PROTEUM2 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0073) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 44.360 | 2.000 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.100 | 0.640 |
| Number of reflections | 10513 | |
| <I/σ(I)> | 26.13 | 2.88 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 30.7 | 15.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 4.5 | 100 MM SODIUM ACETATE, 1 M AMMONIUM DI-HYDROGEN PHOSPHATE, PH 4.5 |






