6P95
Structure of Lassa virus glycoprotein in complex with Fab 25.6A
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-B |
| Synchrotron site | APS |
| Beamline | 23-ID-B |
| Temperature [K] | 80 |
| Detector technology | PIXEL |
| Collection date | 2016-07-17 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 1.033188 |
| Spacegroup name | P 61 2 2 |
| Unit cell lengths | 152.242, 152.242, 453.889 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 29.660 - 3.500 |
| R-factor | 0.2072 |
| Rwork | 0.205 |
| R-free | 0.24720 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5vk2 |
| Data reduction software | XDS |
| Data scaling software | Aimless (0.5.27) |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.15.2_3472) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 29.982 | 3.640 |
| High resolution limit [Å] | 3.500 | 3.500 |
| Rmerge | 0.148 | 1.429 |
| Rmeas | 0.153 | 1.486 |
| Rpim | 0.041 | 0.404 |
| Number of reflections | 40281 | 4448 |
| <I/σ(I)> | 17.4 | |
| Completeness [%] | 99.8 | 100 |
| Redundancy | 13.3 | 13.3 |
| CC(1/2) | 0.999 | 0.683 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 295 | 0.1 M Tris pH 8, 15-18% PEG 3350 and 0.1 M-0.3 M magnesium acetate |






