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 |