1GB5
CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU300 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1999-01-20 |
Detector | RIGAKU RAXIS |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 56.530, 61.040, 32.740 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 1.800 |
R-factor | 0.178 |
Refinement software | X-PLOR |
Data quality characteristics
Overall | |
High resolution limit [Å] | 1.800 |
Rmerge | 0.065 |
Number of reflections | 10271 |
Completeness [%] | 92.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.5 | 283 | drop consists of equal volume of protein and reservoir solutions * |
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) |