1OUI
CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V93A MUTANT
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU RUH3R |
Temperature [K] | 283 |
Detector technology | IMAGE PLATE |
Collection date | 1994-06-28 |
Detector | RIGAKU |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 56.650, 60.850, 33.860 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 1.800 |
R-factor | 0.159 |
Rwork | 0.159 |
RMSD bond length | 0.008 |
RMSD bond angle | 23.955 * |
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 | 0.040 |
Total number of observations | 36666 * |
Number of reflections | 11122 |
Completeness [%] | 98.0 |
Redundancy | 3.29 |
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) |