6CDM
Structure of vaccine-elicited HIV-1 neutralizing antibody vFP7.04 in complex with HIV-1 fusion peptide residue 512-519
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 | 2016-11-17 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 79.565, 61.034, 88.654 |
| Unit cell angles | 90.00, 91.89, 90.00 |
Refinement procedure
| Resolution | 48.417 - 2.408 |
| R-factor | 0.1853 |
| Rwork | 0.183 |
| R-free | 0.22230 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3bky |
| RMSD bond length | 0.005 |
| RMSD bond angle | 0.911 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.440 |
| High resolution limit [Å] | 2.400 | 6.510 | 2.400 |
| Rmerge | 0.127 | 0.054 | 0.412 |
| Rmeas | 0.150 | 0.064 | 0.500 |
| Rpim | 0.079 | 0.034 | 0.279 |
| Total number of observations | 113946 | ||
| Number of reflections | 33013 | 1743 | 1567 |
| <I/σ(I)> | 4.9 | ||
| Completeness [%] | 99.6 | 100 | 95.7 |
| Redundancy | 3.5 | 3.5 | 2.8 |
| CC(1/2) | 0.996 | 0.798 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 293 | 0.1 M MES pH 6.0, 30% PEG 6000 |
