3BPR
Crystal structure of catalytic domain of the proto-oncogene tyrosine-protein kinase MER in complex with inhibitor C52
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 | 2007-03-08 |
| Detector | ADSC QUANTUM 210 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 70.001, 91.702, 120.745 |
| Unit cell angles | 90.00, 94.06, 90.00 |
Refinement procedure
| Resolution | 47.300 - 2.800 |
| R-factor | 0.275 |
| Rwork | 0.274 |
| R-free | 0.30134 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2p0c |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.239 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.900 |
| High resolution limit [Å] | 2.800 | 2.800 |
| Number of reflections | 37537 | |
| <I/σ(I)> | 9.1 | 2.3 |
| Completeness [%] | 99.0 | 94 |
| Redundancy | 3.3 | 2.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8.5 | 287 | Compound C52 (50 mM in DMSO) was added to 8 mg/ml MER protein to the final concentration of 2.5 mM. The mixture was rocked at 277 K overnight and further concentrated to about 35 mg/ml. Crystals were grown by mixing 2 microliters of MER inhibitor solution and 2 microliters of reservoir solution (100 mM Tris-HCl pH 8.5, 3.64 M NaCl) at 287 K using the hanging-drop vapor-diffusion method. Crystals were cryo-protected with a solution composed of glycerol, ethylene glycol, glucose, and fructose., VAPOR DIFFUSION, HANGING DROP, pH 8.50 |
