6FU5
Structure of the kinase domain of human RIPK2 in complex with the inhibitor CSLP18
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | DIAMOND BEAMLINE I04 |
| Synchrotron site | Diamond |
| Beamline | I04 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2017-04-30 |
| Detector | DECTRIS PILATUS 6M-F |
| Wavelength(s) | 0.9795 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 75.790, 122.710, 71.450 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 39.660 - 3.260 |
| R-factor | 0.2313 |
| Rwork | 0.229 |
| R-free | 0.27100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4c8b |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.551 |
| Data reduction software | xia2 |
| Data scaling software | xia2 |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.13_2998: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 39.660 | 3.377 |
| High resolution limit [Å] | 3.260 | 3.260 |
| Number of reflections | 10837 | |
| <I/σ(I)> | 7.12 | |
| Completeness [%] | 99.5 | |
| Redundancy | 6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | 150 nL sitting drops containing 50 nL protein and 100 nL of a reservoir solution containing 0.2 M potassium formate and 20% (w/v) PEG3350 |
