2HLE
Structural and biophysical characterization of the EPHB4-EPHRINB2 protein protein interaction and receptor specificity.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-12-01 |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 41 |
| Unit cell lengths | 81.085, 81.085, 50.945 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.050 |
| R-factor | 0.22928 |
| Rwork | 0.226 |
| R-free | 0.29521 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1kgy |
| RMSD bond length | 0.018 |
| RMSD bond angle | 1.780 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.103 |
| High resolution limit [Å] | 2.050 | 2.050 |
| Number of reflections | 19785 | |
| Completeness [%] | 99.6 | 99.93 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.8 | 293 | 2.2 M Ammonium sulfate, 100 mM Tris, pH 7.8, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
