3FDN
Structure-based drug design of novel Aurora kinase A inhibitors: Structure basis for potency and specificity
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSRRC BEAMLINE BL13B1 |
| Synchrotron site | NSRRC |
| Beamline | BL13B1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-10-19 |
| Detector | ADSC QUANTUM 315 |
| Spacegroup name | P 61 2 2 |
| Unit cell lengths | 81.613, 81.613, 169.145 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 30.000 - 1.900 |
| R-factor | 0.23055 |
| Rwork | 0.228 |
| R-free | 0.28696 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | PDB 1MQ4 |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.413 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP (9.2) |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.970 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.035 | 0.467 |
| Number of reflections | 27121 | |
| <I/σ(I)> | 28.94 | 2.56 |
| Completeness [%] | 98.0 | 99.3 |
| Redundancy | 3.4 | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 291 | 22% PEG400, 0.1mM ammonia sulfate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
