7KQG
Antibodies that engage the hemagglutinin receptor-binding site of influenza B viruses
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 8.2.2 |
Synchrotron site | ALS |
Beamline | 8.2.2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2018-05-23 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.9787 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 40.130, 77.440, 225.650 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 45.600 - 2.600 |
R-factor | 0.2285 |
Rwork | 0.226 |
R-free | 0.28590 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4fqj |
RMSD bond length | 0.005 |
RMSD bond angle | 0.849 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | PHENIX (1.18.2_3874) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 45.600 | 50.000 | 2.700 |
High resolution limit [Å] | 2.600 | 30.000 | 2.600 |
Rmerge | 0.172 | 0.021 | 0.828 |
Rmeas | 0.184 | 0.022 | 0.885 |
Total number of observations | 179861 | ||
Number of reflections | 22576 | 17 | 2376 |
<I/σ(I)> | 12.26 | 42.12 | 2.78 |
Completeness [%] | 99.9 | 94.4 | 100 |
Redundancy | 7.967 | 5.471 | 8.139 |
CC(1/2) | 0.994 | 1.000 | 0.845 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | 100 mM bis-Tris pH 6.5, 20% PEG MME 5000 |