4LSP
Crystal structure of broadly and potently neutralizing antibody VRC-CH31 in complex with HIV-1 clade A/E gp120 93TH057
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 | 2011-06-07 |
Detector | MARMOSAIC 300 mm CCD |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 67.392, 83.958, 175.734 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 48.040 - 2.150 |
R-factor | 0.182 |
Rwork | 0.180 |
R-free | 0.21400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3se9 |
RMSD bond length | 0.005 |
RMSD bond angle | 0.948 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | PHENIX (dev_1317) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.230 |
High resolution limit [Å] | 2.150 | 2.150 |
Rmerge | 0.084 | 0.519 |
Number of reflections | 52604 | |
<I/σ(I)> | 10.8 | |
Completeness [%] | 95.8 | 71.6 |
Redundancy | 5.7 | 2.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 8.5 | 293 | 0.1M Tris, 15% PEG 4000,0.1 M Li2SO4, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |