1JEF
TURKEY LYSOZYME COMPLEX WITH (GLCNAC)3
Experimental procedure
Source type | ROTATING ANODE |
Source details | ELLIOTT GX-21 |
Temperature [K] | 293 |
Detector technology | DIFFRACTOMETER |
Collection date | 1990-02 |
Detector | ENRAF-NONIUS FAST |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 87.490, 32.940, 49.000 |
Unit cell angles | 90.00, 119.10, 90.00 |
Refinement procedure
Resolution | 10.000 - 1.770 |
R-factor | 0.182 |
Rwork | 0.182 |
R-free | 0.22500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | STRUCTURE IN THE NATIVE CRYSTAL |
RMSD bond length | 0.013 |
RMSD bond angle | 2.700 |
Data reduction software | MERGEF |
Data scaling software | MERGEF |
Phasing software | X-PLOR (3.1) |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 23.400 | 1.790 |
High resolution limit [Å] | 1.750 | 1.760 |
Rmerge | 0.058 | 0.225 |
Total number of observations | 50234 * | |
Number of reflections | 10950 | |
Completeness [%] | 86.0 | |
Redundancy | 4.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Microdialysis * | 4.2 | Harata, K., (1993) Acta Crystallogr.,Sect.D, 49, 497. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | ammonium sulfate | 3 (M) | 5 ml |
2 | 1 | 1 | 1-propanol | 10 (%) | 2 ml |
3 | 1 | 1 | sulfric acid | 0.05 (M) | |
4 | 1 | 1 | protein | 100 mg |