2QOC
Human EphA3 kinase domain, phosphorylated, AMP-PNP bound structure
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | CHESS BEAMLINE A1 |
| Synchrotron site | CHESS |
| Beamline | A1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-05-08 |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 0.97900 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 53.790, 38.337, 76.439 |
| Unit cell angles | 90.00, 102.07, 90.00 |
Refinement procedure
| Resolution | 27.450 - 1.250 |
| R-factor | 0.17 |
| Rwork | 0.169 |
| R-free | 0.18600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2qob |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.673 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.290 |
| High resolution limit [Å] | 1.250 | 2.690 | 1.250 |
| Rmerge | 0.050 | 0.039 | 0.250 |
| Number of reflections | 84007 | ||
| <I/σ(I)> | 13.6 | ||
| Completeness [%] | 99.6 | 98.6 | 98.6 |
| Redundancy | 3.6 | 3.5 | 3.3 |
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 |
