3I1L
Structure of porcine torovirus Hemagglutinin-Esterase in complex with its receptor
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-3 |
| Synchrotron site | ESRF |
| Beamline | ID14-3 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-05-13 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.931000 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 156.030, 103.690, 97.070 |
| Unit cell angles | 90.00, 96.02, 90.00 |
Refinement procedure
| Resolution | 46.270 - 2.790 |
| R-factor | 0.1948 |
| Rwork | 0.192 |
| R-free | 0.24285 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3i1k |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.182 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0072) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 48.000 | 2.940 |
| High resolution limit [Å] | 2.790 | 2.790 |
| Rmerge | 0.086 | 0.487 |
| Number of reflections | 36150 | |
| <I/σ(I)> | 10.5 | 2 |
| Completeness [%] | 94.3 | 95.3 |
| Redundancy | 2.7 | 2.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 291 | 0.2M potassium acetate, 18% (w/v) PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 291.0K |
