1OUD
CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V121A MUTANT
Experimental procedure
| Source type | ROTATING ANODE |
| Source details | RIGAKU RUH3R |
| Temperature [K] | 283 |
| Detector technology | IMAGE PLATE |
| Collection date | 1995-11-06 |
| Detector | RIGAKU RAXIS IIC |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 56.770, 60.920, 33.820 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 8.000 - 1.800 |
| R-factor | 0.154 |
| Rwork | 0.154 |
| RMSD bond length | 0.009 |
| RMSD bond angle | 23.991 * |
| Data reduction software | RIGAKU (SOFTWARE) |
| Data scaling software | RIGAKU |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR |
Data quality characteristics
| Overall | |
| High resolution limit [Å] | 1.800 |
| Rmerge | 0.046 |
| Total number of observations | 35004 * |
| Number of reflections | 10733 |
| Completeness [%] | 94.0 |
| Redundancy | 3.26 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 4.5 | 10 * | Takano, K., (1995) J.Mol.Biol., 254, 62. * |
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) |
