1CKG
T52V MUTANT HUMAN LYSOZYME
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU300 |
Temperature [K] | 283 |
Detector technology | IMAGE PLATE |
Collection date | 1998-02-01 |
Detector | RIGAKU RAXIS IIC |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 65.257, 106.667, 39.542 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 2.200 |
Rwork | 0.166 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | WILD-TYPE OF HUMAN LYSOZYME |
RMSD bond length | 0.009 |
RMSD bond angle | 24.900 * |
Data reduction software | PROCESS |
Data scaling software | PROCESS |
Phasing software | AMoRE |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.090 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.100 | 0.239 |
Total number of observations | 31949 * | |
Number of reflections | 16216 | |
<I/σ(I)> | 3.3 | |
Completeness [%] | 83.6 | 61.1 |
Redundancy | 2.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 4.5 * | protein solution is mixed in a 1:1 ratio with well solution * |
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) |