4LST
Crystal structure of broadly and potently neutralizing antibody VRC01 in complex with HIV-1 clade C strain ZM176.66 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 | 2011-01-01 |
Detector | MARMOSAIC 225 mm CCD |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 68.105, 77.981, 200.351 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 40.680 - 2.550 |
R-factor | 0.193 |
Rwork | 0.190 |
R-free | 0.23900 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.004 |
RMSD bond angle | 0.896 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | PHENIX (dev_998) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.590 |
High resolution limit [Å] | 2.550 | 2.550 |
Rmerge | 0.084 | 0.321 |
Number of reflections | 32759 | |
<I/σ(I)> | 10.5 | |
Completeness [%] | 92.0 | 56 |
Redundancy | 3.8 | 3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 8.5 | 293 | 0.1M Tris, 11.8% PEG 4000, 0.2M Na-Acetate , pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |