1B5Z
CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME: CALORIMETRY AND X-RAY ANALYSIS OF SIX SER->ALA MUTANTS
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU RUH3R |
Temperature [K] | 283 |
Detector technology | IMAGE PLATE |
Detector | RIGAKU RAXIS IIC |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 64.670, 110.300, 43.640 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 2.200 |
R-factor | 0.19 * |
Rwork | 0.148 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | I56F MUTANT HUMAN LYSOZYME |
RMSD bond length | 0.009 |
RMSD bond angle | 1.480 |
Data reduction software | PROCESS |
Data scaling software | PROCESS |
Phasing software | X-PLOR (3.1) |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 100.000 | 1.900 |
High resolution limit [Å] | 1.810 | 1.810 |
Rmerge | 0.051 | |
Total number of observations | 68449 * | |
Number of reflections | 23175 | |
<I/σ(I)> | 2.4 | |
Completeness [%] | 79.4 | 52.6 |
Redundancy | 3 |
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) |