1LYY
AMYLOIDOGENIC VARIANT (ASP67HIS) OF HUMAN LYSOZYME
Experimental procedure
| Source type | ROTATING ANODE |
| Source details | RIGAKU |
| Temperature [K] | 288 |
| Detector technology | IMAGE PLATE |
| Collection date | 1995-01 |
| Detector | MARRESEARCH |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 37.340, 31.860, 51.500 |
| Unit cell angles | 90.00, 102.56, 90.00 |
Refinement procedure
| Resolution | 8.000 - 1.800 |
| R-factor | 0.228 |
| Rwork | 0.228 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | HUMAN LYSOZYME COORDINATES FROM ARTYMUIK P.J.AND BLAKE C.C.F. J.MOL.BIOL. (1983) 167 693-723. |
| RMSD bond length | 0.015 |
| RMSD bond angle | 23.100 * |
| 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] | 30.000 | 1.810 |
| High resolution limit [Å] | 1.750 | 1.750 |
| Rmerge | 0.103 | 0.198 |
| Total number of observations | 41333 * | |
| Number of reflections | 11071 | |
| <I/σ(I)> | 8.5 | 3 |
| Completeness [%] | 90.9 | 78.3 |
| Redundancy | 3.7 | 2.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion * | 4 | 20 * | PROTEIN WAS CRYSTALLIZED FROM 0.2 M AMMONIUM SULFATE, 30% PEG 8000, pH 4.0 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | drop | HEPES | 10 (mM) | |
| 3 | 1 | drop | 0.4-0.5 (M) | ||
| 4 | 1 | reservoir | ammonium sulfate | 0.16 (M) | |
| 5 | 1 | reservoir | PEG8000 | 24 (%) |
