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) |
