3KKA
Co-crystal structure of the sam domains of EPHA1 AND EPHA2
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-10-14 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.97932 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 57.554, 56.071, 107.617 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.440 - 2.400 |
| R-factor | 0.2015 |
| Rwork | 0.200 |
| R-free | 0.23463 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3hil |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.392 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 33.000 | 2.440 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Number of reflections | 14362 | |
| <I/σ(I)> | 20.16304 | 2.2083 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 6.9 | 6.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.2 | 293.1 | 2.1 M AMMONIUM SULPHATE, 2% PEG 400, 0.1 M NA HEPES PH 7.2.PRIOR TO SETTING UP CRYSTALLIZATION PLATES, CHYMOTRYPSIN WAS ADDED TO THE PROTEIN SAMPLE TO A FINAL CONCENTRATION OF 0.57 MICROMOLAR., VAPOR DIFFUSION, HANGING DROP, temperature 293.1K |
