5G3U
The structure of the L-tryptophan oxidase VioA from Chromobacterium violaceum in complex with its inhibitor 2-(1H-indol-3-ylmethyl)prop-2- enoic acid
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 | 2014-07-30 |
| Detector | DECTRIS PILATUS 6M |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 69.270, 81.460, 167.120 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 45.983 - 2.377 |
| R-factor | 0.1789 |
| Rwork | 0.177 |
| R-free | 0.21330 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.573 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 45.980 | 2.440 |
| High resolution limit [Å] | 2.380 | 2.380 |
| Rmerge | 0.160 | 0.700 |
| Number of reflections | 38865 | |
| <I/σ(I)> | 11 | 2 |
| Completeness [%] | 100.0 | 99.9 |
| Redundancy | 6.6 | 6.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 290 | 0.1 M HEPES PH 7.0, 10 %(W/V) PEG 6000, 0.1 M LICL, 0.00375 M 2-(1H-INDOL-3-YLMETHYL)PROP-2-ENOIC ACID AT 290 K, THEN SUPPLEMENTED WITH 20 %(V/V) GLYCEROL |
