6FNL
Crystal Structure of Ephrin B4 (EphB4) Receptor Protein Kinase
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 | 2018-01-17 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.918400 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 46.138, 54.061, 62.119 |
| Unit cell angles | 90.00, 110.87, 90.00 |
Refinement procedure
| Resolution | 43.112 - 1.269 |
| R-factor | 0.1968 |
| Rwork | 0.197 |
| R-free | 0.21350 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2vwu |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.834 |
| Data reduction software | XDS (XDSapp 2) |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.10.1_2155)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 43.112 | 1.340 |
| High resolution limit [Å] | 1.269 | 1.269 |
| Rmeas | 0.069 | |
| Number of reflections | 74570 | 11399 |
| <I/σ(I)> | 12.14 | 0.23 |
| Completeness [%] | 97.8 | 93.1 |
| Redundancy | 6.69 | 6.4 |
| CC(1/2) | 0.999 | 0.126 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 291 | 25 % PEG5000 MME, 15 % Glycerol, 0.1 M TRIS pH7.5 |






