1IX0
I59A-3SS human lysozyme
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL40B2 |
Synchrotron site | SPring-8 |
Beamline | BL40B2 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2000-03-27 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 56.830, 60.880, 32.100 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 1.800 |
Rwork | 0.179 |
R-free | 0.25600 * |
Structure solution method | isomorphous |
RMSD bond length | 0.009 * |
RMSD bond angle | 1.490 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | Outer shell | |
High resolution limit [Å] | 1.800 | |
Rmerge | 0.041 * | 0.056 * |
Total number of observations | 50796 * | |
Number of reflections | 10772 | |
Completeness [%] | 99.0 | 98.5 * |
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) |