1LHI
ROLE OF PROLINE RESIDUES IN HUMAN LYSOZYME STABILITY: A SCANNING CALORIMETRIC STUDY COMBINED WITH X-RAY STRUCTURE ANALYSIS OF PROLINE MUTANTS
Experimental procedure
Spacegroup name | P 21 21 21 |
Unit cell lengths | 56.590, 60.710, 33.830 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 5.000 - 1.800 |
R-factor | 0.156 |
RMSD bond length | 0.017 |
RMSD bond angle | 0.037 * |
Refinement software | PROLSQ |
Data quality characteristics
Overall | |
High resolution limit [Å] | 1.800 * |
Rmerge | 0.050 * |
Total number of observations | 25987 * |
Number of reflections | 9952 * |
Completeness [%] | 87.0 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | unknown * | 5.8 * | 13 * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | protein | 20 (mg/ml) | |
2 | 1 | 1 | 2.5 (M) | precipitant | |
3 | 1 | 1 | sodium phosphate | 30 (mM) |