5G3S
The structure of the L-tryptophan oxidase VioA from Chromobacterium violaceum - Samarium derivative
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X06DA |
| Synchrotron site | SLS |
| Beamline | X06DA |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2013-08-22 |
| Detector | DECTRIS PILATUS 2M-F |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 67.880, 87.070, 78.020 |
| Unit cell angles | 90.00, 112.95, 90.00 |
Refinement procedure
| Resolution | 19.984 - 2.076 |
| R-factor | 0.166 |
| Rwork | 0.165 |
| R-free | 0.18810 |
| Structure solution method | SAD |
| Starting model (for MR) | NONE |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.595 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | SHELXCDE |
| Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 19.920 | 2.150 |
| High resolution limit [Å] | 2.080 | 2.080 |
| Rmerge | 0.110 | 0.510 |
| Number of reflections | 49742 | |
| <I/σ(I)> | 26.34 | 6.61 |
| Completeness [%] | 98.0 | 91 |
| Redundancy | 24.4 | 19.6 |
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 THEN SOAKED WITH 0.01 M HGCL2 AND 0.01 M SM(NO3)3 |
