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 |