3HF6
Crystal structure of human tryptophan hydroxylase type 1 with bound LP-521834 and FE
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 4.2.2 |
| Synchrotron site | ALS |
| Beamline | 4.2.2 |
| Detector technology | CCD |
| Detector | NOIR-1 |
| Wavelength(s) | 1.0000 1.5418 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 47.199, 57.893, 55.604 |
| Unit cell angles | 90.00, 93.00, 90.00 |
Refinement procedure
| Resolution | ? - 1.800 |
| Rwork | 0.181 |
| R-free | 0.21683 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 47.130 |
| High resolution limit [Å] | 1.800 |
| Number of reflections | 24850 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 293 | 1:1 ratio of the concentrated protein solution and a reservoir comprising 24-28% (w/v) PEG 6000, and 100 mM, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 20 CK, temperature 293K |
