1JKC
HUMAN LYSOZYME MUTANT WITH TRP 109 REPLACED BY PHE
Experimental procedure
Source type | ROTATING ANODE |
Source details | ENRAF-NONIUS FR571 |
Detector technology | DIFFRACTOMETER |
Detector | ENRAF-NONIUS FAST |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 57.170, 60.830, 32.890 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 1.600 |
R-factor | 0.18 |
Rwork | 0.180 |
R-free | 0.22000 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1lz1 |
RMSD bond length | 0.008 |
RMSD bond angle | 24.368 * |
Data reduction software | MADNES |
Phasing software | X-PLOR |
Refinement software | X-PLOR |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 14.800 |
High resolution limit [Å] | 1.600 |
Rmerge | 0.050 |
Total number of observations | 73731 * |
Number of reflections | 14328 |
Completeness [%] | 91.2 |
Redundancy | 5.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, sitting drop * | 4.5 | Muraki, M.,(1996) Biochemistry, 35, 13562. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | sodium acetate | 25 (mM) | |
2 | 1 | drop | ammonium nitrate | 3 (M) | |
3 | 1 | drop | protein | 20 (mg/ml) | |
4 | 1 | reservoir | sodium acetate | 25 (mM) | |
5 | 1 | reservoir | ammonium nitrate | 5 (M) |