8F12
Structure of the MDM2 P53 binding domain in complex with H103, an all-D Helicon Polypeptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-B |
| Synchrotron site | APS |
| Beamline | 23-ID-B |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2021-03-07 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 1.03317 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 60.310, 60.310, 84.590 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 49.110 - 1.860 |
| R-factor | 0.2162 |
| Rwork | 0.215 |
| R-free | 0.24150 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3g03 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.18.2_3874) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 49.110 | 1.900 |
| High resolution limit [Å] | 1.860 | 1.860 |
| Rmerge | 1.577 | |
| Rmeas | 0.113 | |
| Number of reflections | 13715 | 817 |
| <I/σ(I)> | 18 | |
| Completeness [%] | 99.8 | 98.2 |
| Redundancy | 25.8 | 23.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 291 | 3.2 M Ammonium sulfate, 0.1 M Citrate pH 5.0 |






