1H6A
Reduced Precursor Form of Glucose-Fructose Oxidoreductase from Zymomonas mobilis
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 | 83.896, 93.060, 115.486 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 15.000 - 2.500 |
R-factor | 0.204 |
Rwork | 0.204 |
R-free | 0.27500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ofg |
RMSD bond length | 0.008 |
RMSD bond angle | 23.200 * |
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 | 2.630 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.120 | 0.385 |
Number of reflections | 31238 | |
<I/σ(I)> | 4.2 | 1.9 |
Completeness [%] | 97.9 | 97.3 |
Redundancy | 3.1 | 3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 6.4 * | 12% PEG6000, 210MM AMMONIUM SULFATE, 20% GLYCEROL, 100MM K-SUCCINATE PH6.5, pH 6.50 |
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 | 210 (mM) | |
6 | 1 | reservoir | potassium succinate | 100 (mM) | pH5.5 |