4TWO
Human EphA3 Kinase domain in complex with compound 164
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | BRUKER AXS MICROSTAR |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2010-10-18 |
Detector | MAR scanner 345 mm plate |
Wavelength(s) | 1.54179 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 53.221, 38.068, 75.310 |
Unit cell angles | 90.00, 100.83, 90.00 |
Refinement procedure
Resolution | 30.773 - 2.047 |
R-factor | 0.1646 |
Rwork | 0.163 |
R-free | 0.20060 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2qob |
RMSD bond length | 0.007 |
RMSD bond angle | 0.989 |
Data reduction software | XDS (VERSION January 10, 2014 BUILT=20140115) |
Data scaling software | SCALA (3.3.21) |
Phasing software | PHASER (2.5.6) |
Refinement software | PHENIX ((phenix.refine: 1.9_1692)) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 38.070 | 38.068 | 2.160 |
High resolution limit [Å] | 2.050 | 6.470 | 2.050 |
Rmerge | 0.016 | 0.137 | |
Rmeas | 0.043 | ||
Rpim | 0.026 | 0.013 | 0.099 |
Total number of observations | 49627 | 1557 | 6732 |
Number of reflections | 18078 | ||
<I/σ(I)> | 23 | 55.1 | 8.1 |
Completeness [%] | 95.5 | 94.9 | 90.9 |
Redundancy | 2.7 | 2.5 | 2.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | 0.1M sodium cacodylate pH 6.5, 0.15M ammonium sulfate, 22.5% PEG 3350 |