2QOB
Human EphA3 kinase domain, base structure
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU FR-E+ SUPERBRIGHT |
| Temperature [K] | 200 |
| Detector technology | IMAGE PLATE |
| Collection date | 2006-06-15 |
| Detector | RIGAKU RAXIS IV |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 53.590, 38.098, 76.031 |
| Unit cell angles | 90.00, 101.72, 90.00 |
Refinement procedure
| Resolution | 26.490 - 1.650 |
| R-factor | 0.17 |
| Rwork | 0.169 |
| R-free | 0.19600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2gsf |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.134 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 26.490 | 1.700 |
| High resolution limit [Å] | 1.650 | 1.650 |
| Rmerge | 0.031 | 0.134 |
| Number of reflections | 35314 | |
| <I/σ(I)> | 48.8 | 12.5 |
| Completeness [%] | 95.8 | 64.5 |
| Redundancy | 6.8 | 6.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 298 | 20 mg/mL Protein, 25% PEG 3350, 0.2M Ammonium sulfate, 0.1M Hepes, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
