4NGH
Crystal structure of the HIV-1 neutralizing antibody 4E10 Fab fragment in complex with a hydrocarbon-stapled peptide containing the 4e10 epitope on gp41 and a tethered phosphate moiety.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-B |
| Synchrotron site | APS |
| Beamline | 23-ID-B |
| Temperature [K] | 110 |
| Detector technology | CCD |
| Collection date | 2011-12-10 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.0000 |
| Spacegroup name | P 61 2 2 |
| Unit cell lengths | 226.510, 226.510, 42.330 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 49.040 - 2.680 |
| R-factor | 0.1718 |
| Rwork | 0.169 |
| R-free | 0.22280 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2fx7 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.349 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: 1.7.2_869)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 49.040 | 2.750 |
| High resolution limit [Å] | 2.680 | 2.680 |
| Number of reflections | 18587 | |
| <I/σ(I)> | 28 | 5.6 |
| Completeness [%] | 99.9 | 100 |
| Redundancy | 20.7 | 20.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 295 | Reservoir solution:0.2 M MgCl2, 0.1 M MES pH5.5, 40% PEG 400, VAPOR DIFFUSION, SITTING DROP, temperature 295K |
