6ZJC
Crystal structure of Equus ferus caballus glutathione transferase A3-3 in complex with glutathione and triethyltin
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | DIAMOND BEAMLINE I24 |
Synchrotron site | Diamond |
Beamline | I24 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2020-02-14 |
Detector | DECTRIS PILATUS3 6M |
Wavelength(s) | 0.96852 |
Spacegroup name | P 1 |
Unit cell lengths | 49.401, 54.728, 97.115 |
Unit cell angles | 88.17, 78.74, 86.39 |
Refinement procedure
Resolution | 48.370 - 2.200 |
R-factor | 0.1751 |
Rwork | 0.173 |
R-free | 0.20950 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 6zj9 |
RMSD bond length | 0.012 |
RMSD bond angle | 1.654 |
Data reduction software | DIALS |
Data scaling software | Aimless (0.7.2) |
Phasing software | MOLREP |
Refinement software | REFMAC (5.8.0232) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 48.370 | 48.370 | 2.270 |
High resolution limit [Å] | 2.200 | 9.070 | 2.200 |
Rmerge | 0.119 | 0.045 | 0.442 |
Rmeas | 0.141 | 0.052 | 0.523 |
Rpim | 0.075 | 0.027 | 0.277 |
Total number of observations | 171719 | 2498 | 15066 |
Number of reflections | 49746 | 712 | 4306 |
<I/σ(I)> | 6.4 | 15.1 | 2.5 |
Completeness [%] | 98.4 | 99.4 | 97.4 |
Redundancy | 3.5 | 3.5 | 3.5 |
CC(1/2) | 0.992 | 0.998 | 0.914 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 294 | 0.1 M Bicine/Trizma base pH 8.5, 12.5% (w/v) PEG 1000, 12.5% (w/v) PEG 3350, 12.5% (v/v) MPD, 0.02 M of each monosaccharide (D-glucose, D-mannose, D-galactose, L-fucose, D-xylose, and N-acetyl-D-glucosamine), and 20 mM triethyltin bromide |