2P0C
Catalytic Domain of the Proto-oncogene Tyrosine-protein Kinase MER
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2007-01-23 |
| Detector | RIGAKU RAXIS IV++ |
| Wavelength(s) | 1.54178 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 52.470, 90.057, 69.253 |
| Unit cell angles | 90.00, 102.44, 90.00 |
Refinement procedure
| Resolution | 24.790 - 2.400 |
| R-factor | 0.20761 |
| Rwork | 0.204 |
| R-free | 0.27392 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2g15 |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.201 |
| 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] | 25.000 | 2.490 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Number of reflections | 24544 | |
| <I/σ(I)> | 21.6 | 5.2 |
| Completeness [%] | 99.8 | 99.7 |
| Redundancy | 3.5 | 3.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 298 | The protein in 20mM Tris-HCl pH 8.0, 0.5M NaCl, 5% glycerol, 2mM BME, 2.5 mM AMP-PNP, 10 mM MgCl2, 5mM peptide (ADEPNYETWG) was mixed with crystallization buffer (15% PEG 8000, 0.2M ammonium sulfate, and 0.1 M Sodium cacodylate, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K |
