4H14
Crystal Structure of Bovine Coronavirus Spike Protein Lectin Domain
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 24-ID-E |
| Synchrotron site | APS |
| Beamline | 24-ID-E |
| Wavelength(s) | 0.97918 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 86.563, 86.563, 78.068 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 37.850 - 1.550 |
| R-factor | 0.16334 |
| Rwork | 0.163 |
| R-free | 0.17746 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.005 |
| RMSD bond angle | 0.941 |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 50.010 |
| High resolution limit [Å] | 1.550 |
| Number of reflections | 46536 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | 2.0M (NH4)2SO4, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
