3MH0
Mutagenesis of p38 MAP Kinase eshtablishes key roles of Phe169 in function and structural dynamics and reveals a novel DFG-out state
Replaces: 2PKJExperimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X4A |
| Synchrotron site | NSLS |
| Beamline | X4A |
| Temperature [K] | 93 |
| Detector technology | CCD |
| Collection date | 2004-08-16 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.98 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 68.540, 70.420, 75.660 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 24.560 - 2.000 |
| R-factor | 0.23152 |
| Rwork | 0.227 |
| R-free | 0.28045 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1zyj |
| RMSD bond length | 0.023 |
| RMSD bond angle | 2.018 |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 2.150 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.067 | 0.284 |
| Number of reflections | 25272 | |
| <I/σ(I)> | 4.9 | |
| Completeness [%] | 99.6 | 99.9 |
| Redundancy | 4.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6 | 295 | 10-20% PEG 4000, 0.1 M cacodylic acid, 50 mM n-octyl-beta-D-glucoside, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 295K |
