6F71
Crystal structure of glutathione transferase Omega 6S from Trametes versicolor in complex with naringenin
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM30A |
| Synchrotron site | ESRF |
| Beamline | BM30A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2017-06-23 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9799 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 73.810, 78.880, 93.620 |
| Unit cell angles | 90.00, 101.49, 90.00 |
Refinement procedure
| Resolution | 45.872 - 2.301 |
| R-factor | 0.1689 |
| Rwork | 0.166 |
| R-free | 0.22830 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6f70 |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.243 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | MOLREP |
| Refinement software | PHENIX ((1.10.1_2155: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 49.350 | 2.360 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Rmerge | 0.135 | 0.599 |
| Number of reflections | 46447 | |
| <I/σ(I)> | 8.9 | |
| Completeness [%] | 99.0 | |
| Redundancy | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 278 | 25 % PEG 1500, 0.1 M MMT pH 6.5 buffer (containing DL-malic acid, MES and Tris base in the molar ratios 1:2:2, respectively) |
