1DPX
STRUCTURE OF HEN EGG-WHITE LYSOZYME
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | ENRAF-NONIUS FR591 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Detector | MARRESEARCH |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 77.050, 77.050, 37.210 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 40.000 - 1.650 |
R-factor | 0.1874 * |
Rwork | 0.187 |
R-free | 0.24650 * |
RMSD bond length | 0.010 * |
RMSD bond angle | 2.200 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 99.000 | 1.710 |
High resolution limit [Å] | 1.650 | 1.650 |
Rmerge | 0.038 | 0.143 |
Total number of observations | 176694 * | |
Number of reflections | 13962 | |
<I/σ(I)> | 51 | |
Completeness [%] | 99.7 | 100 |
Redundancy | 12.66 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 * | 293 | SODIUM ACETATE, SODIUM CHLORIDE, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 30 (mg/ml) | |
2 | 1 | reservoir | Tris | 50 (mM) | |
3 | 1 | reservoir | MPD | 70 (%(v/v)) |