3DJ6
Crystal structure of the mouse Aurora-A catalytic domain (Asn186->Gly, Lys240->Arg, Met302->Leu) in complex with Compound 823.
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 | 97.120, 97.120, 62.161 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 30.000 - 1.700 |
| R-factor | 0.21741 |
| Rwork | 0.214 |
| R-free | 0.26092 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2c6d |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.225 |
| 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 | 1.760 |
| High resolution limit [Å] | 1.700 | 1.700 |
| Rmerge | 0.074 | 0.352 |
| Number of reflections | 36636 | |
| <I/σ(I)> | 9.5 | 2 |
| Completeness [%] | 97.7 | 90.3 |
| Redundancy | 3.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 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: 8% tacsimate pH 6.0, 20% PEG 3350; temperature: 293K; cryoprotectant: 20% glycerol; crystal frozen by immersion in liquid nitrogen |
