3NDM
Crystal structure of Rho-Associated Protein Kinase (ROCK1) with a potent isoquinolone derivative
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SLS BEAMLINE X06DA |
Synchrotron site | SLS |
Beamline | X06DA |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2007-05-10 |
Detector | MAR CCD 165 mm |
Wavelength(s) | 1.0 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 162.784, 83.553, 177.962 |
Unit cell angles | 90.00, 119.95, 90.00 |
Refinement procedure
Resolution | 42.527 - 3.300 |
R-factor | 0.244 |
Rwork | 0.241 |
R-free | 0.31050 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.010 |
RMSD bond angle | 1.269 |
Data reduction software | d*TREK |
Data scaling software | d*TREK (9.6L) |
Phasing software | CNX |
Refinement software | PHENIX (1.6.1_357) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 46.950 | 46.950 | 3.420 |
High resolution limit [Å] | 3.300 | 7.100 | 3.300 |
Rmerge | 0.092 | 0.046 | 0.649 |
Number of reflections | 31334 | ||
<I/σ(I)> | 7.4 | 23.6 | 1.7 |
Completeness [%] | 99.6 | 96.2 | 99.7 |
Redundancy | 3.77 | 3.52 | 3.75 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6 | 298 | 8.5% PEG3350, 0.1M MES, 50 mM CaCl2, pH 6.0, vapor diffusion, hanging drop, temperature 298K |