3SE9
Crystal structure of broadly and potently neutralizing antibody VRC-PG04 in complex with HIV-1 gp120
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 | 2010-06-18 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 1 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 61.804, 66.476, 237.305 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 23.734 - 2.000 |
R-factor | 0.1922 |
Rwork | 0.190 |
R-free | 0.23320 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.005 |
RMSD bond angle | 0.917 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | PHENIX ((phenix.refine: dev_755)) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 50.000 |
High resolution limit [Å] | 2.000 |
Number of reflections | 59364 |
Completeness [%] | 88.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | 9.9% PEG 4000, 9.0 % isopropanol, 100 mM Li2SO4, 100 mM HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |