1LZN
NEUTRON STRUCTURE OF HEN EGG-WHITE LYSOZYME
Experimental procedure
Experimental method | LAUE |
Temperature [K] | 295 |
Detector technology | IMAGE PLATE |
Collection date | 1997-12 |
Wavelength(s) | 2.7-3.5 |
Spacegroup name | P 1 |
Unit cell lengths | 27.280, 32.040, 34.270 |
Unit cell angles | 88.80, 108.80, 111.60 |
Refinement procedure
Resolution | 13.600 - 1.700 |
R-factor | 0.204 * |
Rwork | 0.204 |
R-free | 0.22100 |
Structure solution method | MOLECULAR REPLACEMEN XPLOR |
Starting model (for MR) | 4lzt |
RMSD bond length | 0.016 |
RMSD bond angle | 0.033 |
Data reduction software | CCP4 (LAUE SUITE) |
Data scaling software | CCP4 ((LAUE SUITE)) |
Refinement software | CCP4 (LAUE SUITE MODIFIED FOR CYLINDER GEOMETRY (C. WILKINSON)) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 13.600 |
High resolution limit [Å] | 1.700 |
Rmerge | 0.146 |
Total number of observations | 46061 * |
Number of reflections | 8976 |
<I/σ(I)> | 35 |
Completeness [%] | 83.0 |
Redundancy | 3.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Batch method * | 4.7 | BATCH TECHNIQUE EQUAL AMOUNT OF 1.0 % SOLUTION OF HEN EGG-WHITE LYSOZYME ( BOEHRINGER) AND 2.8 % NANO3 IN 50 MM ACETATE BUFFER (PH 4.7) |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | protein | 1.0 (%) | |
2 | 1 | 1 | 2.8 (%) | ||
3 | 1 | 1 | acetate | 50 (mM) |