3DJ5
Crystal structure of the mouse Aurora-A catalytic domain (Asn186->Gly, Lys240->Arg, Met302->Leu) in complex with Compound 290.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL7-1 |
| Synchrotron site | SSRL |
| Beamline | BL7-1 |
| Temperature [K] | 160 |
| Detector technology | CCD |
| Collection date | 2008-04-29 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.98 |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 97.738, 97.738, 62.224 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 30.000 - 1.800 |
| R-factor | 0.2099 |
| Rwork | 0.207 |
| R-free | 0.24299 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2c6d |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.166 |
| 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 | 1.860 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.053 | 0.167 |
| Number of reflections | 31664 | |
| <I/σ(I)> | 16.6 | 4.9 |
| Completeness [%] | 98.7 | 99.8 |
| Redundancy | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 5.6 | 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: 0.1 M sodium citrate tribasic dihydrate pH 5.6, 2% tacsimate, 16% PEG 3350; temperature: 293K; cryoprotectant: 20% glycerol; crystal frozen by immersion in liquid nitrogen |
