5LDE
Crystal structure of a vFLIP-IKKgamma stapled peptide dimer
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SOLEIL BEAMLINE PROXIMA 1 |
| Synchrotron site | SOLEIL |
| Beamline | PROXIMA 1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-04-07 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9790 |
| Spacegroup name | P 63 |
| Unit cell lengths | 90.510, 90.510, 134.780 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 25.000 - 3.380 |
| R-factor | 0.257 |
| Rwork | 0.255 |
| R-free | 0.29000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3cl3 |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.030 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | BUSTER (2.10.2) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 78.500 | 3.560 |
| High resolution limit [Å] | 3.300 | 3.300 |
| Rmerge | 0.110 | 1.773 |
| Rpim | 0.902 | |
| Number of reflections | 9482 | 1954 |
| <I/σ(I)> | 10.3 | 1.3 |
| Completeness [%] | 99.8 | |
| Redundancy | 9.4 | 9.6 |
| CC(1/2) | 0.498 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 299 | 1.2M Ammonium Sulphate, 0.05M tri-sodium citrate, 3% isopropanol, 0.1-0.2% vitamin B12 |
