1H6D
Oxidized 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 1 21 1 |
Unit cell lengths | 115.724, 83.752, 279.149 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 15.000 - 2.050 |
R-factor | 0.197 |
Rwork | 0.197 |
R-free | 0.22800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ofg |
RMSD bond length | 0.006 |
RMSD bond angle | 23.700 * |
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 | 2.160 |
High resolution limit [Å] | 2.050 | 2.050 |
Rmerge | 0.094 | 0.388 |
Number of reflections | 317883 | |
<I/σ(I)> | 6.2 | 1.8 |
Completeness [%] | 99.9 | 99.9 |
Redundancy | 3.8 | 3.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 6 | 12% PEG6000, 550MM AMMONIUM SULFATE, 20% GLYCEROL, pH 6.00 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 20 (mg/ml) | |
2 | 1 | drop | MES/KOH | 40 (mM) | pH6.4 |
3 | 1 | reservoir | PEG6000 | 12 (%) | |
4 | 1 | reservoir | glycerol | 20 (%) | |
5 | 1 | reservoir | ammonium sulfate | 550 (mM) |