7ZIF
Crystal structure of human tryptophan hydroxylase 1 in complex with inhibitor KM-480
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | BESSY BEAMLINE 14.1 |
| Synchrotron site | BESSY |
| Beamline | 14.1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2014-01-28 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.9184 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 47.021, 57.919, 59.416 |
| Unit cell angles | 90.00, 97.65, 90.00 |
Refinement procedure
| Resolution | 41.293 - 1.869 |
| R-factor | 0.161484691984 |
| Rwork | 0.160 |
| R-free | 0.19881 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1mlw |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.260 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 41.293 | 1.940 |
| High resolution limit [Å] | 1.869 | 1.870 |
| Rmerge | 0.070 | 0.443 |
| Number of reflections | 26286 | 2564 |
| <I/σ(I)> | 14.53 | |
| Completeness [%] | 99.8 | 98.69 |
| Redundancy | 4.1 | 3.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293.15 | 8% w/v PEG 8000, 100 mM Tris-HCl pH 8.5 |
