1IOC
CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME, EAEA-I56T
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PHOTON FACTORY BEAMLINE BL-18B |
Synchrotron site | Photon Factory |
Beamline | BL-18B |
Temperature [K] | 100 |
Detector technology | DIFFRACTOMETER |
Collection date | 1999-11-27 |
Detector | WEISSENBERG |
Wavelength(s) | 1 |
Spacegroup name | P 61 2 2 |
Unit cell lengths | 90.120, 90.120, 92.640 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 6.000 - 2.400 |
R-factor | 0.21 |
Rwork | 0.210 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | EAEA human lysozyme |
Data reduction software | DENZO |
Phasing software | X-PLOR |
Refinement software | X-PLOR |
Data quality characteristics
Overall | |
High resolution limit [Å] | 2.400 |
Rmerge | 0.118 |
Total number of observations | 72930 * |
Number of reflections | 9168 |
Completeness [%] | 99.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.6 | 10 * | Goda, S., (2000) Protein Eng., 13, 299. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 15 (mg/ml) | |
2 | 1 | reservoir | cadmium chloride | 0.1 (M) | |
3 | 1 | reservoir | sodium acetate | 0.1 (M) | |
4 | 1 | reservoir | PEG400 | 30 (%(v/v)) |