3FXX
Human EphA3 Kinase and Juxtamembrane Region Bound to Substrate KQWDNYE[pTyr]IW
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU FR-E+ SUPERBRIGHT |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2007-02-06 |
| Detector | RIGAKU RAXIS IV |
| Wavelength(s) | 1.54178 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 53.463, 38.201, 76.649 |
| Unit cell angles | 90.00, 102.15, 90.00 |
Refinement procedure
| Resolution | 26.470 - 1.700 |
| R-factor | 0.168 |
| Rwork | 0.166 |
| R-free | 0.19400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2gsf |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.279 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 30.000 | 30.000 | 1.760 |
| High resolution limit [Å] | 1.700 | 3.660 | 1.700 |
| Rmerge | 0.044 | 0.032 | 0.312 |
| Number of reflections | 33335 | ||
| <I/σ(I)> | 28.359 | ||
| Completeness [%] | 98.3 | 99.9 | 84.1 |
| Redundancy | 3.4 | 3.6 | 2.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 298 | 20 mg/mL Protein, 25% PEG 3350, 0.04M Ammonium sulfate, 0.1M Tris, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K |






