7ZII
Crystal structure of human tryptophan hydroxylase 1 in complex with inhibitor KM-05-193
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 | 2015-07-19 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 0.9184 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 46.970, 57.947, 59.349 |
Unit cell angles | 90.00, 97.62, 90.00 |
Refinement procedure
Resolution | 29.552 - 1.628 |
R-factor | 0.168344186808 |
Rwork | 0.167 |
R-free | 0.19191 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1mlw |
RMSD bond length | 0.009 |
RMSD bond angle | 1.199 |
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] | 29.552 | 1.690 |
High resolution limit [Å] | 1.628 | 1.630 |
Rmerge | 0.067 | 0.724 |
Number of reflections | 39546 | 3859 |
<I/σ(I)> | 14.71 | |
Completeness [%] | 99.7 | |
Redundancy | 4.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293.15 | 20% w/v PEG 3350, 200 mM potassium formate pH 7.3 |