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 300 mm |
| 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 |
