2QOO
Human EphA3 kinase and juxtamembrane region, Y596F:Y602F:Y742F triple 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 | 54.111, 38.255, 75.975 |
| Unit cell angles | 90.00, 102.24, 90.00 |
Refinement procedure
| Resolution | 26.440 - 1.250 |
| R-factor | 0.19 |
| Rwork | 0.189 |
| R-free | 0.20200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2gsf |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.107 |
| 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 | 1.290 |
| High resolution limit [Å] | 1.250 | 2.690 | 1.250 |
| Rmerge | 0.035 | 0.021 | 0.630 |
| Number of reflections | 83007 | ||
| <I/σ(I)> | 13.2 | ||
| Completeness [%] | 98.4 | 97.5 | 88.7 |
| Redundancy | 4 | 4 | 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 |
