5AR7
RIP2 Kinase Catalytic Domain (1 - 310) complex with Biaryl Urea
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 | 2009-02-08 |
| Detector | ADSC CCD |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 131.600, 131.600, 107.540 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 34.130 - 2.710 |
| R-factor | 0.1836 |
| Rwork | 0.181 |
| R-free | 0.22520 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5ar4 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.100 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | REFMAC |
| Refinement software | BUSTER (2.11.5) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 80.000 | 2.860 |
| High resolution limit [Å] | 2.710 | 2.710 |
| Rmerge | 0.090 | 0.350 |
| Number of reflections | 29605 | |
| <I/σ(I)> | 10.2 | 3.1 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 4.1 | 4.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6.5 | 30% PEG300, 0.1M MES PH6.5 |
