5EJB
Crystal structure of prefusion Hendra virus F protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.2.2 |
| Synchrotron site | ALS |
| Beamline | 8.2.2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-08-25 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.99969 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 108.610, 163.500, 147.940 |
| Unit cell angles | 90.00, 94.13, 90.00 |
Refinement procedure
| Resolution | 49.620 - 3.200 |
| R-factor | 0.2542 |
| Rwork | 0.253 |
| R-free | 0.28330 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2b9b |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.541 |
| Data reduction software | XDS (January 10, 2014) |
| Data scaling software | XDS (January 10, 2014) |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0073) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 49.620 | 3.280 |
| High resolution limit [Å] | 3.200 | 3.200 |
| Rmerge | 0.122 | 0.666 |
| Number of reflections | 80411 | |
| <I/σ(I)> | 8.37 | 1.9 |
| Completeness [%] | 99.6 | 99.6 |
| Redundancy | 3.99 | 4.07 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5 | 295 | 100mM sodium acetate pH 5.0, 1.75M lithium sulfate, 100mM magnesium sulfate, 3.4 % isopropanol |
