1YAO
CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: CALORIMETRIC STUDIES AND X-RAY STRUCTURAL ANALYSIS OF THE FIVE ISOLEUCINE TO VALINE MUTANTS
Experimental procedure
| Detector technology | IMAGE PLATE |
| Detector | RIGAKU RAXIS IIC |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 56.708, 60.854, 33.724 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 8.000 - 1.800 |
| R-factor | 0.16 |
| Rwork | 0.160 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.470 |
| Data reduction software | PROCESS |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR |
Data quality characteristics
| Overall | |
| High resolution limit [Å] | 1.580 * |
| Rmerge | 0.057 |
| Total number of observations | 49674 * |
| Number of reflections | 15567 |
| Completeness [%] | 94.1 |
| Redundancy | 3.19 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 4.5 * | 10 * |
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) |
