1REM
HUMAN LYSOZYME WITH MAN-B1,4-GLCNAC COVALENTLY ATTACHED TO ASP53
Experimental procedure
Detector technology | IMAGE PLATE |
Detector | RIGAKU RAXIS IIC |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 36.390, 116.380, 30.910 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 2.100 |
R-factor | 0.168 |
Rwork | 0.168 |
R-free | 0.24800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1REY EXCEPT RESIDUE NAG 131 |
RMSD bond length | 0.011 |
RMSD bond angle | 24.225 * |
Data reduction software | R-AXIS (SOFTWARE 2.1) |
Data scaling software | R-AXIS (IIC V. 2.1) |
Phasing software | X-PLOR (3.1) |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 36.400 |
High resolution limit [Å] | 2.070 |
Rmerge | 0.057 |
Total number of observations | 22724 * |
Number of reflections | 7438 |
Completeness [%] | 94.9 |
Redundancy | 3.05 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, sitting drop * | 4.5 | Muraki, M., (1991) Biochim. Biophys. Acta 1079, 229. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | sodium acetate | 25 (mM) | |
2 | 1 | drop | ammonium nitrate | 3 (M) | |
3 | 1 | drop | protein | 20 (mg/ml) | |
4 | 1 | reservoir | sodium acetate | 25 (mM) | |
5 | 1 | reservoir | ammonium nitrate | 5 (M) |