4P5Z
Human EphA3 Kinase domain in complex with quinoxaline derivatives
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X06SA |
| Synchrotron site | SLS |
| Beamline | X06SA |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2013-02-22 |
| Detector | PSI PILATUS 6M |
| Wavelength(s) | 0.99989 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 52.805, 38.235, 75.465 |
| Unit cell angles | 90.00, 101.46, 90.00 |
Refinement procedure
| Resolution | 47.018 - 2.002 |
| R-factor | 0.1805 |
| Rwork | 0.178 |
| R-free | 0.21850 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2qob |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.658 |
| Data reduction software | XDS (20140115) |
| Data scaling software | SCALA (3.3.20) |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: 1.8.4_1496)) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 73.960 | 47.018 | 2.110 |
| High resolution limit [Å] | 2.002 | 6.330 | 2.000 |
| Rmerge | 0.029 | 0.586 | |
| Rmeas | 0.075 | ||
| Rpim | 0.029 | 0.012 | 0.245 |
| Total number of observations | 130503 | 4147 | 18334 |
| Number of reflections | 20066 | ||
| <I/σ(I)> | 15.6 | 43.9 | 3 |
| Completeness [%] | 99.1 | 99.1 | 96.2 |
| Redundancy | 6.5 | 6 | 6.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | 0.1M sodium cacodylate pH 6.5, 0.15M ammonium sulfate, 22.5% PEG 3350 |
