8F10
Structure of the MDM2 P53 binding domain in complex with H102, an all-D Helicon Polypeptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS-II BEAMLINE 17-ID-2 |
Synchrotron site | NSLS-II |
Beamline | 17-ID-2 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2021-03-18 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.97933 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 28.150, 39.920, 42.360 |
Unit cell angles | 90.00, 95.44, 90.00 |
Refinement procedure
Resolution | 28.020 - 1.280 |
R-factor | 0.1546 |
Rwork | 0.154 |
R-free | 0.16690 |
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] | 42.170 | 1.300 |
High resolution limit [Å] | 1.280 | 1.280 |
Rmerge | 0.049 | 0.420 |
Number of reflections | 20614 | 233 |
<I/σ(I)> | 18.2 | 2.1 |
Completeness [%] | 85.3 | |
Redundancy | 4.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 291 | 0.01 M tri-Sodium citrate, 33 % w/v PEG 6000 |