1GER
THE STRUCTURE OF GLUTATHIONE REDUCTASE FROM ESCHERICHIA COLI AT 1.86 ANGSTROMS RESOLUTION: COMPARISON WITH THE ENZYME FROM HUMAN ERYTHROCYTES
Experimental procedure
Spacegroup name | P 1 1 21 |
Unit cell lengths | 120.500, 73.600, 60.500 |
Unit cell angles | 90.00, 90.00, 83.00 |
Refinement procedure
Resolution | 7.000 - 1.860 |
R-factor | 0.168 |
Rwork | 0.168 |
RMSD bond length | 0.016 |
RMSD bond angle | 2.830 |
Phasing software | X-PLOR |
Refinement software | X-PLOR |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 9999.000 * | |
High resolution limit [Å] | 1.860 * | |
Rmerge | 0.091 * | |
Number of reflections | 83086 * | |
Completeness [%] | 95.1 * | 78.3 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 5.5 * | 20 * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 15-30 (mg/ml) | |
2 | 1 | drop | potassium phosphate | 100 (mM) | |
3 | 1 | drop | PEG8000 | 7 (%) | |
4 | 1 | drop | 0.02 (%) | ||
5 | 1 | reservoir | potassium phosphate | 100 (mM) | |
6 | 1 | reservoir | PEG8000 | 20 (%) |