5IA3
Crystal Structure of Ephrin A2 (EphA2) Receptor Protein Kinase with PD173955
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X06DA |
| Synchrotron site | SLS |
| Beamline | X06DA |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2015-02-07 |
| Detector | DECTRIS PILATUS 2M |
| Wavelength(s) | 0.85506 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 32.766, 107.543, 40.534 |
| Unit cell angles | 90.00, 108.68, 90.00 |
Refinement procedure
| Resolution | 53.772 - 1.788 |
| R-factor | 0.1629 |
| Rwork | 0.161 |
| R-free | 0.20360 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1mqb |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.891 |
| Data reduction software | XDS |
| Data scaling software | autoPROC |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.10.1_2155: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 53.772 | 1.794 |
| High resolution limit [Å] | 1.788 | 1.788 |
| Rmerge | 0.139 | 0.960 |
| Number of reflections | 24769 | |
| <I/σ(I)> | 9.51 | |
| Completeness [%] | 98.0 | |
| Redundancy | 3.56 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 291 | 37.5 % MPD_P1k_P3350, 0.2 M Amino Acids, 0.1 M Buffer3 pH 8.5 |






