5G3T
The structure of the L-tryptophan oxidase VioA from Chromobacterium violaceum
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PETRA III, DESY BEAMLINE P11 |
| Synchrotron site | PETRA III, DESY |
| Beamline | P11 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2013-06-25 |
| Detector | DECTRIS PILATUS 6M |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 68.090, 89.160, 144.430 |
| Unit cell angles | 90.00, 92.66, 90.00 |
Refinement procedure
| Resolution | 19.992 - 1.800 |
| R-factor | 0.1585 |
| Rwork | 0.157 |
| R-free | 0.19220 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | NONE |
| RMSD bond length | 0.008 |
| RMSD bond angle | 0.935 |
| 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] | 19.980 | 1.850 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.100 | 0.950 |
| Number of reflections | 157109 | |
| <I/σ(I)> | 10.91 | 2 |
| Completeness [%] | 98.0 | 97.3 |
| Redundancy | 6.9 | 6.94 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8.5 | 277 | 0.08 M TRIS PH 8.5, 24 %(W/V) PEG 4000, 0.16 M MGCL2, 20 %(V/V) GLYCEROL AT 277 K |
