1B4F
OLIGOMERIC STRUCTURE OF THE HUMAN EPHB2 RECEPTOR SAM DOMAIN
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 5.0.2 |
| Synchrotron site | ALS |
| Beamline | 5.0.2 |
| Temperature [K] | 100 |
| Collection date | 1998-08 |
| Wavelength(s) | 0.96859, 0.97966, 0.97982, 1.0000 |
| Spacegroup name | P 41 |
| Unit cell lengths | 73.897, 73.897, 104.547 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 26.000 - 1.950 |
| R-factor | 0.228 |
| Rwork | 0.228 |
| R-free | 0.27300 |
| Structure solution method | MAD |
| RMSD bond length | 0.028 |
| RMSD bond angle | 22.100 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CNS (0.4) |
| Refinement software | CNS (0.4) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 26.000 | 2.020 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Rmerge | 0.047 * | 0.163 * |
| Total number of observations | 223269 * | |
| Number of reflections | 39547 | |
| <I/σ(I)> | 17.6 | 6.84 |
| Completeness [%] | 96.5 | 98.7 |
| Redundancy | 5.6 | 5.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7 | 4 * | pH 7.0 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 20 (mg/ml) | |
| 2 | 1 | reservoir | HEPES | 100 (mM) | |
| 3 | 1 | reservoir | Tris | 10 (mM) | |
| 4 | 1 | reservoir | dithiothreitol | 20 (mM) | |
| 5 | 1 | reservoir | 30 (mM) | ||
| 6 | 1 | reservoir | PEG1000 | 26-30 (%) |
