3D15
Crystal structure of mouse Aurora A (Asn186->Gly, Lys240->Arg, Met302->Leu) in complex with 1-(3-chloro-phenyl)-3-{5-[2-(thieno[3,2-d]pyrimidin-4-ylamino)- ethyl]-thiazol-2-yl}-urea [SNS-314]
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL7-1 |
Synchrotron site | SSRL |
Beamline | BL7-1 |
Temperature [K] | 180 |
Detector technology | CCD |
Collection date | 2008-04-28 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.98 |
Spacegroup name | P 61 2 2 |
Unit cell lengths | 82.353, 82.353, 171.999 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 20.000 - 2.300 |
R-factor | 0.23752 |
Rwork | 0.234 |
R-free | 0.28750 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1mq4 |
RMSD bond length | 0.009 |
RMSD bond angle | 1.330 |
Data reduction software | CrystalClear |
Data scaling software | d*TREK |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.400 |
High resolution limit [Å] | 2.300 | 2.300 |
Rmerge | 0.046 | 0.396 |
Number of reflections | 15885 | |
<I/σ(I)> | 17.3 | 3.3 |
Completeness [%] | 99.1 | 100 |
Redundancy | 5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 293 | Protein at 8.5 mg/ml in 50 mM Tris pH 7.0, 200 mM NaCl, 3 mM DTT, hanging-drop, vapor diffusion, mother liquor:bis-Tris propane ph 7.0, 35% tacsimate, temperature:293K, cryoprotectant:tacsimate, crystal frozen by immersion in liquid nitrogen |