4JAN
crystal structure of broadly neutralizing antibody CH103 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 | 2012-07-22 |
Detector | MAR CCD 300MM |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 48.943, 208.651, 69.422 |
Unit cell angles | 90.00, 107.21, 90.00 |
Refinement procedure
Resolution | 46.750 - 3.150 |
R-factor | 0.199 |
Rwork | 0.196 |
R-free | 0.25600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3ngb |
RMSD bond length | 0.002 |
RMSD bond angle | 0.610 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | PHENIX ((phenix.refine: 1.8_1069)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 3.250 |
High resolution limit [Å] | 3.150 | 3.210 |
Rmerge | 0.360 | |
Number of reflections | 20488 | |
<I/σ(I)> | 10 | 2.3 |
Completeness [%] | 89.4 | 59 |
Redundancy | 3.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7.5 | 293 | 200 mM sodium formate, 20% PEG 3350 and 100 mM Bistrispropane, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |