1CKG
T52V MUTANT HUMAN LYSOZYME
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU300 |
| Temperature [K] | 283 |
| Detector technology | IMAGE PLATE |
| Collection date | 1998-02-01 |
| Detector | RIGAKU RAXIS IIC |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 65.257, 106.667, 39.542 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 8.000 - 2.200 |
| Rwork | 0.166 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | WILD-TYPE OF HUMAN LYSOZYME |
| RMSD bond length | 0.009 |
| RMSD bond angle | 24.900 * |
| Data reduction software | PROCESS |
| Data scaling software | PROCESS |
| Phasing software | AMoRE |
| Refinement software | X-PLOR (3.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.090 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.100 | 0.239 |
| Total number of observations | 31949 * | |
| Number of reflections | 16216 | |
| <I/σ(I)> | 3.3 | |
| Completeness [%] | 83.6 | 61.1 |
| Redundancy | 2.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 4.5 * | protein solution is mixed in a 1:1 ratio with well solution * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | reservoir | 2.5 (M) | ||
| 3 | 1 | reservoir | acetate | 20 (mM) |






