4CHS
Crystal structure of a tau class glutathione transferase 10 from Glycine max
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X13 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X13 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-11-06 |
| Detector | MAR CCD 165 mm |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 47.670, 90.860, 112.900 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.659 - 1.600 |
| R-factor | 0.1632 |
| Rwork | 0.162 |
| R-free | 0.19390 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3FHS |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.390 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHASER |
| Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.700 |
| High resolution limit [Å] | 1.600 | 1.600 |
| Rmerge | 0.040 | 0.040 |
| Number of reflections | 65115 | |
| Completeness [%] | 99.5 | 98.9 |
| Redundancy | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7 | PEG 3350 22% (W/V), MGCL2 0.2 M, BIS-TRIS 0.1 M, PH 5.6 |
