1LOZ
AMYLOIDOGENIC VARIANT (I56T) VARIANT OF HUMAN LYSOZYME
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 288 |
Detector technology | IMAGE PLATE |
Collection date | 1995-02 |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 56.847, 60.889, 33.699 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 1.800 |
R-factor | 0.211 * |
Rwork | 0.211 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1LZM |
RMSD bond length | 0.013 |
RMSD bond angle | 24.500 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | X-PLOR (3.1) |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 15.000 | 1.860 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.092 | 0.240 |
Total number of observations | 49524 * | |
Number of reflections | 10578 | |
<I/σ(I)> | 11.2 | 3.6 |
Completeness [%] | 92.8 | 87.2 |
Redundancy | 4.7 | 2.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 4 | THE PROTEIN WAS CRYSTALLIZED FROM 0.16M AMMONIUM SULFATE, 24% PEG 8000 BY VAPOR DIFFUSION., pH 4.0, vapor diffusion |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 5 (mg/ml) | |
2 | 1 | drop | HEPES | 5 (mM) | |
3 | 1 | drop | 0.2-0.25 (M) | ||
4 | 1 | drop | ammonium sulfate | 0.08 (M) | |
5 | 1 | drop | PEG8000 | 12 (%) | |
6 | 1 | reservoir | ammonium sulfate | 0.16 (M) | |
7 | 1 | reservoir | PEG8000 | 24 (%) |