4L0P
Structure of the human EphA3 receptor ligand binding domain complexed with ephrin-A5
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-B |
| Synchrotron site | APS |
| Beamline | 23-ID-B |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2012-10-21 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.03320 |
| Spacegroup name | P 43 |
| Unit cell lengths | 60.043, 60.043, 91.574 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 38.518 - 2.260 |
| R-factor | 0.1879 |
| Rwork | 0.187 |
| R-free | 0.21110 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | The ephrin-A5 subunit from PDB entry 1SHW |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.785 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | AutoSol |
| Refinement software | PHENIX ((phenix.refine: 1.8.1_1168)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.340 |
| High resolution limit [Å] | 2.260 | 2.260 |
| Rmerge | 0.190 | 0.839 |
| Number of reflections | 15094 | |
| <I/σ(I)> | 7.9 | 1.6 |
| Completeness [%] | 98.7 | 97.6 |
| Redundancy | 5.2 | 4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8 | 292 | 2.05M ammonium sulphate, 0.1M tris, 5mM calcium chloride, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 292K |
