1ADS
AN UNLIKELY SUGAR SUBSTRATE SITE IN THE 1.65 ANGSTROMS STRUCTURE OF THE HUMAN ALDOSE REDUCTASE HOLOENZYME IMPLICATED IN DIABETIC COMPLICATIONS
Experimental procedure
Spacegroup name | P 21 21 21 |
Unit cell lengths | 50.000, 67.120, 92.020 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 10.000 - 1.650 |
R-factor | 0.2 |
Rwork | 0.200 |
RMSD bond length | 0.014 |
RMSD bond angle | 3.130 |
Phasing software | X-PLOR |
Refinement software | X-PLOR |
Data quality characteristics
Overall | |
High resolution limit [Å] | 1.650 * |
Rmerge | 0.045 * |
Total number of observations | 128951 * |
Number of reflections | 35859 * |
Completeness [%] | 92.7 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 5 * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 14 (mg/ml) | |
2 | 1 | drop | citrate | 50 (mM) | |
3 | 1 | drop | beta-mercaptoethanol | 7 (mM) | |
4 | 1 | drop | PEG6000 | in various concentrations | |
5 | 1 | reservoir | PEG | 20 (%) | |
6 | 1 | reservoir | citrate | 50 (mM) |