4P4C
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 | 53.914, 38.164, 75.527 |
| Unit cell angles | 90.00, 101.59, 90.00 |
Refinement procedure
| Resolution | 33.643 - 1.599 |
| R-factor | 0.1793 |
| Rwork | 0.178 |
| R-free | 0.20170 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2gsf |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.343 |
| Data scaling software | SCALA (3.3.16) |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: 1.8.4_1496)) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 38.164 | 38.164 | 1.690 |
| High resolution limit [Å] | 1.599 | 5.060 | 1.599 |
| Rmerge | 0.029 | 0.317 | |
| Rmeas | 0.061 | ||
| Rpim | 0.032 | 0.018 | 0.195 |
| Total number of observations | 138288 | 4130 | 20222 |
| Number of reflections | 39425 | ||
| <I/σ(I)> | 13.9 | 31.6 | 3.7 |
| Completeness [%] | 98.2 | 92.5 | 97.6 |
| Redundancy | 3.5 | 3.3 | 3.5 |
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 |
