3RCD
HER2 Kinase Domain Complexed with TAK-285
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-D |
| Synchrotron site | APS |
| Beamline | 23-ID-D |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2007-08-17 |
| Detector | MAR scanner 300 mm plate |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 1 |
| Unit cell lengths | 50.542, 64.936, 92.360 |
| Unit cell angles | 90.42, 89.72, 90.35 |
Refinement procedure
| Resolution | 40.000 - 3.210 |
| R-factor | 0.22729 |
| Rwork | 0.224 |
| R-free | 0.29352 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3pp0 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.235 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC |
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 | 0.083 | 0.036 | 0.211 |
| Number of reflections | 14548 | ||
| <I/σ(I)> | 8.3 | ||
| Completeness [%] | 76.3 | 95.8 | 42.6 |
| Redundancy | 1.7 | 1.9 | 1.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 298 | 20% PEG 3550, 200MM DI-AMMONIUM TARTRATE, 100 MM PIPES, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
