5AR2
RIP2 Kinase Catalytic Domain (1 - 310)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-11-04 |
| Detector | ADSC CCD |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 132.566, 132.566, 107.788 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 20.000 - 2.440 |
| R-factor | 0.17189 |
| Rwork | 0.170 |
| R-free | 0.21125 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | NONE |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.358 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | REFMAC |
| Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 75.000 | 2.570 |
| High resolution limit [Å] | 2.440 | 2.440 |
| Rmerge | 0.070 | 0.380 |
| Number of reflections | 41021 | |
| <I/σ(I)> | 12.6 | 3.6 |
| Completeness [%] | 99.9 | 100 |
| Redundancy | 4.2 | 4.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7.5 | 28% PEG400, 5% GLYCEROL, 0.1M HEPES PH7.5, 0.2M CACL2 |
