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 |