7Y55
Crystal structure of a glutathione S-transferase Tau1 from Pinus densata in complex with GSH
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRF BEAMLINE BL19U1 |
Synchrotron site | SSRF |
Beamline | BL19U1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2021-05-14 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 0.979 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 166.402, 55.509, 119.754 |
Unit cell angles | 90.00, 112.50, 90.00 |
Refinement procedure
Resolution | 38.434 - 2.191 |
R-factor | 0.276769379248 |
Rwork | 0.276 |
R-free | 0.30209 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4top |
RMSD bond length | 0.008 |
RMSD bond angle | 1.235 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | PHENIX |
Refinement software | PHENIX (1.9_1692+SVN) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 10.000 | 2.230 |
High resolution limit [Å] | 2.190 | 5.940 | 2.190 |
Rmerge | 0.167 | 0.151 | 0.703 |
Rmeas | 0.182 | 0.165 | 0.811 |
Rpim | 0.073 | 0.065 | 0.389 |
Total number of observations | 275021 | ||
Number of reflections | 49207 | 2718 | 1717 |
<I/σ(I)> | 3.3 | ||
Completeness [%] | 94.5 | 99.7 | 66.6 |
Redundancy | 5.6 | 6.3 | 3.3 |
CC(1/2) | 0.968 | 0.742 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 289 | 0.1 M MES monohydrate pH 5.5, 25% v/v Polyethylene glycol 400 |