4UMN
Structure of a stapled peptide antagonist bound to Nutlin-resistant Mdm2.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSRRC |
Synchrotron site | NSRRC |
Temperature [K] | 100 |
Collection date | 2014-04-07 |
Spacegroup name | P 2 21 21 |
Unit cell lengths | 39.076, 65.674, 105.683 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 105.680 - 1.990 |
R-factor | 0.2023 |
Rwork | 0.200 |
R-free | 0.23683 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2axi |
RMSD bond length | 0.005 |
RMSD bond angle | 1.260 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0069) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.020 |
High resolution limit [Å] | 1.970 | 1.970 |
Rmerge | 0.050 | 0.340 |
Number of reflections | 19576 | |
<I/σ(I)> | 34.74 | 4.87 |
Completeness [%] | 99.3 | 95.3 |
Redundancy | 6.4 | 5.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.4 | 289 | 0.04 M CITRIC ACID, 0.06 M BIS-TRIS PROPANE PH 6.4, AND 20% PEG 3350 |