5WCC
Crystal structure of the broadly neutralizing Influenza A antibody VRC 315 02-1F07 Fab.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 22-ID |
Synchrotron site | APS |
Beamline | 22-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2016-12-09 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 1 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 179.217, 70.581, 94.543 |
Unit cell angles | 90.00, 111.86, 90.00 |
Refinement procedure
Resolution | 46.624 - 2.461 |
R-factor | 0.2048 |
Rwork | 0.203 |
R-free | 0.24040 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5ty6 |
RMSD bond length | 0.002 |
RMSD bond angle | 0.586 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | PHENIX (1.12_2829) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 46.624 | 2.540 |
High resolution limit [Å] | 2.450 | 2.450 |
Rmerge | 0.161 | 0.861 |
Number of reflections | 39756 | |
<I/σ(I)> | 11.56 | |
Completeness [%] | 100.0 | |
Redundancy | 5.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 293 | 40% (w/v) PEG-400, 11% (w/v) PEG-8000, 0.1 M Tris, pH 8.8 |