3SE8
Crystal structure of broadly and potently neutralizing antibody VRC03 in complex with HIV-1 gp120
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 22-BM |
Synchrotron site | APS |
Beamline | 22-BM |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-01-01 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 1 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 62.010, 70.259, 217.879 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 37.032 - 1.895 |
R-factor | 0.1893 |
Rwork | 0.187 |
R-free | 0.23280 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.005 |
RMSD bond angle | 0.971 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | PHENIX ((phenix.refine: dev_755)) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 50.000 |
High resolution limit [Å] | 1.895 |
Number of reflections | 69237 |
Completeness [%] | 90.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 293 | 9 % PEG 4000, 200 mM Li2SO4, 100 mM Tris/Cl-, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |