5DDL
Crystal Structure of WT Human Glutathione Transferase Pi soaked with a metalloid then back-soaked with glutathione
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX1 |
Synchrotron site | Australian Synchrotron |
Beamline | MX1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2015-07-23 |
Detector | ADSC QUANTUM 210r |
Wavelength(s) | 0.96 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 77.665, 89.795, 68.854 |
Unit cell angles | 90.00, 98.08, 90.00 |
Refinement procedure
Resolution | 37.496 - 1.980 |
R-factor | 0.1401 |
Rwork | 0.138 |
R-free | 0.17800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5gss |
RMSD bond length | 0.012 |
RMSD bond angle | 1.346 |
Data scaling software | Aimless (0.3.11) |
Phasing software | PHASER (2.5.3) |
Refinement software | PHENIX ((phenix.refine: 1.8.2_1309)) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 46.900 | 46.900 | 2.030 |
High resolution limit [Å] | 1.980 | 9.070 | 1.980 |
Rmerge | 0.061 | 0.027 | 0.286 |
Rpim | 0.016 | 0.008 | 0.079 |
Total number of observations | 488857 | 4784 | 30648 |
Number of reflections | 32553 | ||
<I/σ(I)> | 27 | 64.1 | 7.4 |
Completeness [%] | 99.9 | 99.1 | 98.8 |
Redundancy | 15 | 13.2 | 13.7 |
CC(1/2) | 1.000 | 1.000 | 0.978 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6 | 293 | 100MM MES, PH 6.0, 28% (W/V) PEG 8000, 20MM CACL2, 10MM DTT. Soaked in 2mM PAO dissolved in DMSO, Then back soaked in 10mM GSH after 2 days |