1KKE
Crystal Structure of Reovirus Attachment Protein Sigma1 Trimer
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU300 |
Temperature [K] | 293 |
Detector technology | IMAGE PLATE |
Collection date | 2001-02-01 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.541789 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 52.700, 89.000, 119.800 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.600 |
Rwork | 0.172 |
R-free | 0.23500 * |
Structure solution method | MIR |
RMSD bond length | 0.006 |
RMSD bond angle | 1.400 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | MLPHARE |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.700 |
High resolution limit [Å] | 2.600 | 2.600 |
Rmerge | 0.087 | 0.284 |
Total number of observations | 56260 * | |
Number of reflections | 16338 | |
<I/σ(I)> | 9 | 2.2 |
Completeness [%] | 91.0 | 64 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 7.5 | 20 * | PEG4000, Isopropanol, Hepes, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 6 (mg/ml) | |
2 | 1 | reservoir | isopropanol | 10 (%) | |
3 | 1 | reservoir | PEG4000 | 20 (%) | |
4 | 1 | reservoir | HEPES | 100 (mM) | pH7.5 |