1IAN
HUMAN P38 MAP KINASE INHIBITOR COMPLEX
Experimental procedure
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X4A |
Synchrotron site | NSLS |
Beamline | X4A |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1996-08-31 |
Detector | FUJI |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 65.100, 74.300, 77.900 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 6.000 - 2.000 |
R-factor | 0.234 |
Rwork | 0.234 |
R-free | 0.30100 |
Structure solution method | SE-MET MAD AND MR |
Starting model (for MR) | ERK2 |
RMSD bond length | 0.009 |
RMSD bond angle | 24.100 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | MADSYS |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.100 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.046 | 0.157 |
Total number of observations | 179632 * | |
Number of reflections | 25453 | |
<I/σ(I)> | 23 | 7 |
Completeness [%] | 99.0 | 95 |
Redundancy | 7 | 5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 7.4 | 21-25 * | Pav, S., (1997) Protein Sci., 6, 242. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | enzyme | 6.0 (mg/ml) | |
2 | 1 | drop | inhibitor | 1.4 (mM) | |
3 | 1 | reservoir | PEG1500 | 28-32 (%(w/v)) | |
4 | 1 | reservoir | dithiothreitol | 5 (mM) |