1B0D
Structural effects of monovalent anions on polymorphic lysozyme crystals
Experimental procedure
Experimental method | MONOCHROMATIC |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 293 |
Detector technology | IMAGE PLATE |
Collection date | 1994-04-01 |
Detector | RIGAKU RAXIS II |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 79.060, 79.060, 37.970 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 14.000 - 1.840 |
Rwork | 0.202 |
R-free | 0.24100 |
Structure solution method | OTHER |
RMSD bond length | 0.008 * |
RMSD bond angle | 1.320 * |
Data reduction software | MOSFLM |
Data scaling software | CCP4 |
Phasing software | CCP4 |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 13.500 | 1.900 |
High resolution limit [Å] | 1.850 | 1.850 |
Rmerge | 0.049 * | 0.135 * |
Number of reflections | 10484 * | |
<I/σ(I)> | 10.5 | 4.5 |
Completeness [%] | 97.5 | 85.8 |
Redundancy | 6.6 | 4.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.5 | 291 | 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 | deionized lysozyme | 40.4 (mg/ml) | |
2 | 1 | drop | 50 (mM) | ||
3 | 1 | reservoir | NapTS | 90 (mM) | |
4 | 1 | reservoir | 50 (mM) |