4XUF
Crystal structure of the FLT3 kinase domain bound to the inhibitor quizartinib (AC220)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.2.2 |
| Synchrotron site | ALS |
| Beamline | 8.2.2 |
| Temperature [K] | 80 |
| Detector technology | CCD |
| Collection date | 2014-09-10 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.000 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 48.726, 75.492, 153.968 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 46.455 - 3.200 |
| R-factor | 0.2992 |
| Rwork | 0.297 |
| R-free | 0.32040 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1rjb |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.874 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHENIX |
| Refinement software | PHENIX ((phenix.refine: dev_1839)) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 3.310 |
| High resolution limit [Å] | 3.200 | 6.890 | 3.200 |
| Rmerge | 0.209 | 0.120 | 0.597 |
| Rmeas | 0.248 | 0.144 | 0.717 |
| Rpim | 0.131 | 0.078 | 0.390 |
| Total number of observations | 32682 | ||
| Number of reflections | 9403 | ||
| <I/σ(I)> | 5.3 | ||
| Completeness [%] | 94.3 | 99.5 | 77.1 |
| Redundancy | 3.5 | 3.5 | 2.9 |
| CC(1/2) | 0.980 | 0.698 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 294 | 0.1 M Tris-HCl, pH 7.5, 32% PEG 3350 |
