1H6B
Reduced Precursor Form of Glucose-Fructose Oxidoreductase from Zymomonas mobilis complexed with glycerol
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU300 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Detector | MAR scanner 345 mm plate |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 83.800, 92.774, 115.447 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 15.000 - 2.600 |
R-factor | 0.2 |
Rwork | 0.200 |
R-free | 0.25200 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ofg |
RMSD bond length | 0.008 |
RMSD bond angle | 23.600 * |
Data reduction software | DENZO |
Data scaling software | SCALA |
Phasing software | AMoRE |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 15.000 | 2.740 |
High resolution limit [Å] | 2.600 | 2.600 |
Rmerge | 0.104 | 0.312 |
Number of reflections | 27470 | |
<I/σ(I)> | 6.1 | 2.4 |
Completeness [%] | 96.9 | 83.9 |
Redundancy | 5.8 | 3.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 6.4 * | 16% PEG6000, 5% GLYCEROL, 100MM K-SUCCINATE PH6.5, 1.5M SORBITOL, pH 6.50 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 5 (mg/ml) | |
2 | 1 | drop | MES/KOH | 40 (mM) | pH6.4 |
3 | 1 | reservoir | PEG6000 | 16 (%) | |
4 | 1 | reservoir | potassium succinate | 100 (mM) | pH6.5 |
5 | 1 | reservoir | glycerol | 5 (%) | |
6 | 1 | reservoir | sorbitol | 1.5 (M) |