6A4K
Human antibody 32D6 Fab in complex with H1N1 influenza A virus HA1
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSRRC BEAMLINE TPS 05A |
| Synchrotron site | NSRRC |
| Beamline | TPS 05A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2017-06-12 |
| Detector | RAYONIX MX300-HS |
| Wavelength(s) | 1.0000 |
| Spacegroup name | P 31 1 2 |
| Unit cell lengths | 181.743, 181.743, 248.091 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 20.000 - 3.150 |
| R-factor | 0.17792 |
| Rwork | 0.175 |
| R-free | 0.23287 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3gbn 3n9g |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.532 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 3.260 |
| High resolution limit [Å] | 3.150 | 3.150 |
| Rmerge | 0.077 | 0.554 |
| Number of reflections | 79824 | 7965 |
| <I/σ(I)> | 14.7 | 2.1 |
| Completeness [%] | 98.6 | 99.3 |
| Redundancy | 3.2 | 3.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | 14%(w/v) PEG 8000, 160mM Calcium acetate, 20%(v/v) glycerol, 80mM Sodium Cacodylate, Hydrochloric acid |
