5CHY
STRUCTURE OF CHEMOTAXIS PROTEIN CHEY
Experimental procedure
Source type | ROTATING ANODE |
Temperature [K] | 292 |
Detector technology | IMAGE PLATE |
Detector | RIGAKU RAXIS II |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 45.600, 46.550, 53.330 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 10.000 - 2.000 |
R-factor | 0.185 * |
Rwork | 0.185 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.012 |
RMSD bond angle | 0.044 |
Data reduction software | RIGAKU |
Data scaling software | RIGAKU |
Refinement software | PROFFT |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 2.130 | |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.066 | |
Total number of observations | 21022 * | |
Number of reflections | 7433 | |
<I/σ(I)> | 1 | |
Completeness [%] | 92.0 | 80.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 6 | 4 * | 28% PEG 8000, 0.12 M CALCIUM ACETATE, 0.1 M CACODYLATE BUFFER, PH 6.0 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | PEG8000 | 28 (%) | |
2 | 1 | reservoir | calcium acetate | 0.12 (M) | |
3 | 1 | reservoir | cacodylate | 0.1 (M) |