1LJR
GLUTATHIONE TRANSFERASE (HGST T2-2) FROM HUMAN
Experimental procedure
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE BW7B |
Synchrotron site | EMBL/DESY, HAMBURG |
Beamline | BW7B |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1996-10 |
Detector | MARRESEARCH |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 94.350, 94.350, 120.170 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 15.000 - 3.200 |
R-factor | 0.208 |
Rwork | 0.208 |
R-free | 0.30600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | L. CUPRINA GST |
RMSD bond length | 0.008 |
RMSD bond angle | 24.900 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | X-PLOR (3.8) |
Refinement software | X-PLOR (3.8) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 3.300 |
High resolution limit [Å] | 3.200 | 3.200 |
Rmerge | 0.148 * | |
Total number of observations | 27540 * | |
Number of reflections | 10111 | |
<I/σ(I)> | 7.4 | 3.1 |
Completeness [%] | 96.0 | 97.8 |
Redundancy | 2.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7 * | 277 or 295 * | drop solution was mixed with an equal volume of reservoir solution * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 1.76 (mg/ml) | |
2 | 1 | drop | sodium phosphate | 10 (mM) | |
3 | 1 | drop | beta-mercaptoethanol | 1 (mM) | |
4 | 1 | reservoir | PEG4000 | 15 (%) | |
5 | 1 | reservoir | ethanol | 2 (%) | |
6 | 1 | reservoir | HEPES | 100 (mM) |