3FYJ
Crystal structure of an optimzied benzothiophene inhibitor bound to MAPKAP Kinase-2 (MK-2)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 17-ID |
| Synchrotron site | APS |
| Beamline | 17-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-03-13 |
| Detector | ADSC |
| Wavelength(s) | 1.00 |
| Spacegroup name | F 41 3 2 |
| Unit cell lengths | 255.551, 255.551, 255.551 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 29.510 - 3.800 |
| R-factor | 0.33074 |
| Rwork | 0.328 |
| R-free | 0.38827 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2p3g |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.539 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 29.510 | 30.000 | 3.830 |
| High resolution limit [Å] | 3.700 | 7.930 | 3.700 |
| Rmerge | 0.084 | 0.049 | 0.370 |
| Number of reflections | 6885 | ||
| <I/σ(I)> | 18.664 | ||
| Completeness [%] | 85.6 | 69.1 | 90.5 |
| Redundancy | 5.1 | 4.7 | 5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.4 | 298 | MK-2 protein at 5 mg/ml is equilibrated against a well solution of 1.6 - 2.0 M Sodium malonate at pH 5.4, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
