207L
MUTANT HUMAN LYSOZYME C77A
Experimental procedure
Source type | ROTATING ANODE |
Source details | OTHER |
Temperature [K] | 280 |
Detector technology | IMAGE PLATE |
Collection date | 1993-02-01 |
Detector | MACSCIENCE |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 57.640, 60.700, 32.970 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 6.000 - 1.800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | NATIVE HUMAN LYSOZYME |
RMSD bond length | 0.014 |
RMSD bond angle | 0.036 |
Data reduction software | PROTEIN |
Data scaling software | PROTEIN |
Phasing software | PROTEIN |
Refinement software | PROLSQ |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 100.000 | 1.780 |
High resolution limit [Å] | 1.750 | 1.750 |
Rmerge | 0.074 | |
Number of reflections | 8903 | |
Completeness [%] | 75.3 | 42.2 |
Redundancy | 2.68 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 4 * | 4 * | pH 6.0 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 20.0 (mg/ml) | |
2 | 1 | drop | 1.8 (M) | ||
3 | 1 | drop | sodium phosphate | 30 (mM) | |
4 | 1 | reservoir | 2.0 (M) | ||
5 | 1 | reservoir | sodium phosphate | 30 (mM) |