5IA2
Crystal Structure of Ephrin A2 (EphA2) Receptor Protein Kinase with compound 66
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | BESSY BEAMLINE 14.1 |
| Synchrotron site | BESSY |
| Beamline | 14.1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2015-07-15 |
| Detector | PSI PILATUS 6M |
| Wavelength(s) | 0.918409 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 32.864, 107.517, 40.731 |
| Unit cell angles | 90.00, 108.84, 90.00 |
Refinement procedure
| Resolution | 53.758 - 1.619 |
| R-factor | 0.1643 |
| Rwork | 0.163 |
| R-free | 0.19880 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1mqb |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.868 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.10.1_2155: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 53.758 | 1.624 |
| High resolution limit [Å] | 1.619 | 1.619 |
| Rmerge | 0.070 | 0.537 |
| Number of reflections | 33944 | |
| <I/σ(I)> | 12.7 | |
| Completeness [%] | 99.7 | |
| Redundancy | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 291 | 37.5 % MPD_P1k_P3350, 0.1 M Amino Acids, 0.1 M MES pH 7.0 |
