3E2T
The catalytic domain of chicken tryptophan hydroxylase 1 with bound tryptophan
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-3 |
| Synchrotron site | ESRF |
| Beamline | ID14-3 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-08-27 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.934 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 78.000, 155.300, 61.800 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 48.340 - 1.900 |
| R-factor | 0.184 |
| Rwork | 0.182 |
| R-free | 0.22600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1pah |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.275 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | MOLREP |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 48.340 | 2.000 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.145 | 0.789 |
| Number of reflections | 30024 | 4233 |
| <I/σ(I)> | 13.84 | 2.6 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 7.2 | 7.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 277 | 0.2M imidazole malate, 22.5% PEG 10000, pH 8.5, vapor diffusion, sitting drop, temperature 277K |
