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 |