4Q5Q
Crystal Structure of the Glutathione S-transferase Der p 8
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 22-ID |
Synchrotron site | APS |
Beamline | 22-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2013-03-14 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 1.0 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 72.619, 75.558, 79.366 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 34.823 - 1.931 |
R-factor | 0.1804 |
Rwork | 0.178 |
R-free | 0.22690 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2dc5 |
RMSD bond length | 0.006 |
RMSD bond angle | 0.950 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MLPHARE |
Refinement software | PHENIX ((phenix.refine: 1.8.2_1309)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.960 |
High resolution limit [Å] | 1.930 | 1.930 |
Number of reflections | 31759 | |
<I/σ(I)> | 7 | 2.3 |
Completeness [%] | 95.1 | 85.5 |
Redundancy | 4.9 | 3.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | Cacodylate, Magnesium Acetate, PEG4000, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |