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 |