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) |