7S8H
Structure of Lassa virus glycoprotein bound to Fab 18.5C and Fab 36.1F
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 23-ID-D |
Synchrotron site | APS |
Beamline | 23-ID-D |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2018-04-19 |
Detector | DECTRIS PILATUS3 6M |
Wavelength(s) | 1.033190 |
Spacegroup name | P 3 2 1 |
Unit cell lengths | 163.058, 163.058, 173.548 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 47.180 - 2.700 |
Rwork | 0.217 |
R-free | 0.25080 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 6p91 |
RMSD bond length | 0.005 |
RMSD bond angle | 0.764 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHENIX |
Refinement software | PHENIX (1.19.2_4158) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 47.180 | 2.800 |
High resolution limit [Å] | 2.700 | 2.700 |
Number of reflections | 73503 | 7267 |
<I/σ(I)> | 9.53 | |
Completeness [%] | 99.9 | |
Redundancy | 10 | |
CC(1/2) | 0.996 | 0.260 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 293.15 | 0.1 M Tris, pH 8.0, 1.25 M LiCl and 15% PEG 8k |