1REZ
HUMAN LYSOZYME-N-ACETYLLACTOSAMINE COMPLEX
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 | 58.410, 60.710, 32.840 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 8.000 - 1.700 |
| R-factor | 0.169 |
| Rwork | 0.169 |
| R-free | 0.21500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | NATIVE HUMAN LYSOZYME (PDB ENTRY 1LZ1) |
| RMSD bond length | 0.009 |
| RMSD bond angle | 24.660 * |
| Data reduction software | MADNES |
| Phasing software | X-PLOR (3.1) |
| Refinement software | X-PLOR (3.1) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 14.700 |
| High resolution limit [Å] | 1.610 |
| Rmerge | 0.049 |
| Number of reflections | 12070 |
| Completeness [%] | 76.9 |
| Redundancy | 1.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, sitting drop * | 4.5 | Muraki, M., (1991) Biochim. Biophys. Acta 1079, 229. * |
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) |
