1OUA
CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE I56T MUTANT
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU RUH3R |
Temperature [K] | 283 |
Detector technology | IMAGE PLATE |
Collection date | 1996-04-23 |
Detector | RIGAKU |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 56.690, 61.030, 33.790 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 1.800 |
R-factor | 0.148 |
Rwork | 0.148 |
Structure solution method | DIFFERENCE FOURIER |
RMSD bond length | 0.009 |
RMSD bond angle | 24.159 * |
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 | 0.056 |
Total number of observations | 28187 * |
Number of reflections | 9220 |
Completeness [%] | 80.4 |
Redundancy | 3.05 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 4.5 | 10 * | pH 4.5 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | 2.2 (M) | ||
2 | 1 | reservoir | acetate | 20 (mM) | |
3 | 1 | drop | protein | 5.6 (mg/ml) |