5LK1
Structure of hantavirus envelope glycoprotein Gc in postfusion conformation in presence of 200 mM KCL
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2013-09-07 |
| Detector | DECTRIS PILATUS3 S 6M |
| Wavelength(s) | 0.976251 |
| Spacegroup name | H 3 |
| Unit cell lengths | 107.289, 107.289, 127.539 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 37.550 - 1.700 |
| R-factor | 0.1786 |
| Rwork | 0.177 |
| R-free | 0.20320 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5ljz |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.287 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 37.550 | 1.730 |
| High resolution limit [Å] | 1.700 | 1.700 |
| Rmerge | 0.061 | 0.217 |
| Number of reflections | 56962 | |
| <I/σ(I)> | 9.3 | 3 |
| Completeness [%] | 94.5 | 91.1 |
| Redundancy | 2.3 | 2.2 |
| CC(1/2) | 0.994 | 0.840 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 291 | 0.1M MES 6.5, 10.77%(v/v) PEG 8000, 7% (v/v) glycerol, 200 mM KCl |
