1GUL
HUMAN GLUTATHIONE TRANSFERASE A4-4 COMPLEX WITH IODOBENZYL GLUTATHIONE
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL9-1 |
Synchrotron site | SSRL |
Beamline | BL9-1 |
Temperature [K] | 77 |
Detector technology | IMAGE PLATE |
Collection date | 1997-04-17 |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 155.300, 156.100, 101.300 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 160.000 - 2.700 |
R-factor | 0.25 |
Rwork | 0.248 |
R-free | 0.26000 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1gse |
RMSD bond length | 0.019 |
RMSD bond angle | 2.770 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | TNT (5E) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 9999.000 * | 2.800 |
High resolution limit [Å] | 2.700 | 2.700 |
Rmerge | 0.110 * | |
Number of reflections | 58800 * | |
<I/σ(I)> | 12.9 | 3.5 |
Completeness [%] | 86.0 | 99.8 |
Redundancy | 8.7 | 3.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 7 | CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM 20% PEG 4000, 100 MM PH 7.0, THEN SOAKED IN 1MM IODOBENZYL GLUTATHIONE |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | PEG6000 | 10 (%(w/v)) | |
2 | 1 | reservoir | HEPES | 100 (mM) |