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 |