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 (%) |