4FQY
Crystal structure of broadly neutralizing antibody CR9114 bound to H3 influenza hemagglutinin
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] | 100 |
Detector technology | CCD |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 1.033 |
Spacegroup name | I 21 3 |
Unit cell lengths | 203.710, 203.710, 203.710 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 48.015 - 5.253 |
R-factor | 0.3661 |
Rwork | 0.366 |
R-free | 0.37400 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.010 |
RMSD bond angle | 1.281 |
Data reduction software | HKL-2000 |
Phasing software | PHASER |
Refinement software | PHENIX ((phenix.refine: 1.8_1069)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 5.350 |
High resolution limit [Å] | 5.250 | 5.250 |
Number of reflections | 5386 | |
<I/σ(I)> | 27.3 | 2 |
Completeness [%] | 99.7 | 99.3 |
Redundancy | 20.2 | 9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 4 | 293 | 200 mM zinc acetate, 14% PEG1000, 100 mM sodium acetate, pH 4.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K |