1MQB
Crystal Structure of Ephrin A2 (ephA2) Receptor Protein Kinase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 5.0.3 |
| Synchrotron site | ALS |
| Beamline | 5.0.3 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2001-12-12 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 72.127, 72.127, 241.623 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 63.000 * - 2.300 |
| R-factor | 0.23619 |
| Rwork | 0.236 |
| R-free | 0.28900 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1jpa |
| RMSD bond length | 0.021 * |
| RMSD bond angle | 2.110 * |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.1.19) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 63.000 * | 2.360 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Rmerge | 0.057 | 0.485 |
| Number of reflections | 35483 | |
| <I/σ(I)> | 11.5 | 2 |
| Completeness [%] | 95.0 * | 78 * |
| Redundancy | 4.1 | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.6 * | 4 * | Ethylene Glycol, PEG 10K, HEPES, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10.7 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 50 (mM) | pH7.6 |
| 3 | 1 | drop | 250 (mM) | ||
| 4 | 1 | drop | EDTA | 1 (mM) | |
| 5 | 1 | drop | dithiothreitol | 1 (mM) | |
| 6 | 1 | reservoir | HEPES | 0.1 (M) | pH7.5 |
| 7 | 1 | reservoir | PEG10000 | 10 (%) | |
| 8 | 1 | reservoir | ethylene glycol | 8 (%) |
