1PME
STRUCTURE OF PENTA MUTANT HUMAN ERK2 MAP KINASE COMPLEXED WITH A SPECIFIC INHIBITOR OF HUMAN P38 MAP KINASE
Experimental procedure
| Source type | ROTATING ANODE |
| Source details | RIGAKU |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1997-02 |
| Detector | RIGAKU |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 48.640, 69.680, 60.280 |
| Unit cell angles | 90.00, 109.25, 90.00 |
Refinement procedure
| Resolution | 6.000 - 2.000 |
| R-factor | 0.212 |
| Rwork | 0.212 |
| R-free | 0.27300 |
| RMSD bond length | 0.007 |
| RMSD bond angle | 23.500 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | X-PLOR (3.8) |
| Refinement software | X-PLOR (3.8) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 30.000 |
| High resolution limit [Å] | 1.800 |
| Rmerge | 0.031 |
| Number of reflections | 30531 |
| Completeness [%] | 86.2 |
| Redundancy | 2.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion * | 7 | drop solution was mixed with an equal volume of reservoir solution * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 14 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 20 (mM) | |
| 3 | 1 | drop | dithiothreitol | 5 (mM) | |
| 4 | 1 | drop | 200 (mM) | ||
| 5 | 1 | reservoir | HEPES | 100 (mM) | |
| 6 | 1 | reservoir | mPEG2000 | 28-30 (%(v/v)) | |
| 7 | 1 | reservoir | ammonium sulfate | 200 (mM) | |
| 8 | 1 | reservoir | beta-ME | 20 (mM) |
