5EVM
Crystal Structure of Nipah Virus Fusion Glycoprotein in the Prefusion State
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 24-ID-C |
| Synchrotron site | APS |
| Beamline | 24-ID-C |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2011-03-01 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.9792 |
| Spacegroup name | H 3 |
| Unit cell lengths | 355.750, 355.750, 168.859 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 43.158 - 3.367 |
| R-factor | 0.2136 |
| Rwork | 0.213 |
| R-free | 0.21990 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2b9b |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.521 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 3.470 |
| High resolution limit [Å] | 3.350 | 3.350 |
| Rmerge | 0.161 | 0.975 |
| Number of reflections | 112120 | |
| <I/σ(I)> | 2.41 | 2.41 |
| Completeness [%] | 99.4 | 93.93 |
| Redundancy | 5.9 | 5.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.3 | 298 | 0.1 M HEPES, 1% Jeffamine ED-2001, 1.2 M sodium malonate |
