5NG3
Structure of inactive kinase RIP2K(K47R)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2015-03-15 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.972 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 77.022, 103.310, 204.299 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 92.160 - 2.600 |
| R-factor | 0.2335 |
| Rwork | 0.232 |
| R-free | 0.26869 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5ng0 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.425 |
| Data reduction software | iMOSFLM |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 92.160 | 2.690 |
| High resolution limit [Å] | 2.600 | 2.600 |
| Rmerge | 0.128 | 0.902 |
| Rmeas | 0.154 | 1.147 |
| Rpim | 0.102 | 0.700 |
| Number of reflections | 47644 | |
| <I/σ(I)> | 6.5 | |
| Completeness [%] | 98.6 | |
| Redundancy | 4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | 0.1 M Tris pH 8.5, 0.5 mM (NH4)2SO4 |
