1DLA
NOVEL NADPH-BINDING DOMAIN REVEALED BY THE CRYSTAL STRUCTURE OF ALDOSE REDUCTASE
Experimental procedure
Spacegroup name | P 1 |
Unit cell lengths | 81.300, 85.900, 56.600 |
Unit cell angles | 102.30, 103.30, 79.00 |
Refinement procedure
Resolution | ? - 3.000 |
R-factor | 0.219 |
Rwork | 0.219 |
RMSD bond length | 0.020 |
RMSD bond angle | 3.700 |
Phasing software | X-PLOR |
Refinement software | X-PLOR |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 82.000 * |
High resolution limit [Å] | 2.500 * |
Rmerge | 0.065 * |
Total number of observations | 128597 * |
Number of reflections | 40833 * |
Completeness [%] | 82.0 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 6.2 * | 4 * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | enzyme | 5 (mg/ml) | |
2 | 1 | drop | PEG6000 | 2.5 (%(w/v)) | |
3 | 1 | drop | citrate | 10 (mM) | |
4 | 1 | drop | dithiothreitol | 1 (mM) | |
5 | 1 | drop | sodium azide | 1 (mM) | |
6 | 1 | reservoir | PEG6000 | 20 (%(w/v)) |