4P4C
Human EphA3 Kinase domain in complex with quinoxaline derivatives
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SLS BEAMLINE X06SA |
Synchrotron site | SLS |
Beamline | X06SA |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2013-02-22 |
Detector | PSI PILATUS 6M |
Wavelength(s) | 0.99989 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 53.914, 38.164, 75.527 |
Unit cell angles | 90.00, 101.59, 90.00 |
Refinement procedure
Resolution | 33.643 - 1.599 |
R-factor | 0.1793 |
Rwork | 0.178 |
R-free | 0.20170 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2gsf |
RMSD bond length | 0.009 |
RMSD bond angle | 1.343 |
Data scaling software | SCALA (3.3.16) |
Phasing software | PHASER |
Refinement software | PHENIX ((phenix.refine: 1.8.4_1496)) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 38.164 | 38.164 | 1.690 |
High resolution limit [Å] | 1.599 | 5.060 | 1.599 |
Rmerge | 0.029 | 0.317 | |
Rmeas | 0.061 | ||
Rpim | 0.032 | 0.018 | 0.195 |
Total number of observations | 138288 | 4130 | 20222 |
Number of reflections | 39425 | ||
<I/σ(I)> | 13.9 | 31.6 | 3.7 |
Completeness [%] | 98.2 | 92.5 | 97.6 |
Redundancy | 3.5 | 3.3 | 3.5 |
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 |