2WET
Crystal structure of tryptophan 5-halogenase (PyrH) complex with FAD (tryptophan)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SRS BEAMLINE PX10.1 |
| Synchrotron site | SRS |
| Beamline | PX10.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | MARRESEARCH |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 137.530, 137.530, 307.830 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 48.060 - 2.400 |
| R-factor | 0.19817 |
| Rwork | 0.196 |
| R-free | 0.23380 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2aqj |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.320 |
| Data reduction software | MOSFLM |
| Data scaling software | MOSFLM |
| Refinement software | REFMAC (5.5.0070) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.530 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Rmerge | 0.090 | 0.340 |
| Number of reflections | 113154 | |
| <I/σ(I)> | 16.9 | 3.7 |
| Completeness [%] | 97.6 | 92.4 |
| Redundancy | 7 | 4.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6.2 | 0.05M SODIUM CACODYLATE BUFFER PH6.2, 1.4M LI2SO4 0.01M MGCL2 |
