2QOD
Human EphA3 kinase and juxtamembrane region, Y602F mutant
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 | 2006-10-22 |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 1.00000 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 54.215, 38.289, 76.004 |
| Unit cell angles | 90.00, 102.43, 90.00 |
Refinement procedure
| Resolution | 23.400 - 1.150 |
| R-factor | 0.193 |
| Rwork | 0.192 |
| R-free | 0.20600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2gsf |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.139 |
| 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] | 40.000 | 40.000 | 1.190 |
| High resolution limit [Å] | 1.150 | 2.480 | 1.150 |
| Rmerge | 0.036 | 0.024 | 0.625 |
| Number of reflections | 107783 | ||
| <I/σ(I)> | 13.2 | ||
| Completeness [%] | 99.5 | 95.8 | 99.7 |
| Redundancy | 3.9 | 3.9 | 3.6 |
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 |
