5DT1
Crystal structure of human Fab CAP256-VRC26.25, a potent V1V2-directed HIV-1 broadly neutralizing antibody
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 | 2014-11-26 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 21 2 21 |
| Unit cell lengths | 77.016, 77.027, 85.227 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 42.614 - 1.954 |
| R-factor | 0.1716 |
| Rwork | 0.169 |
| R-free | 0.21460 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4od1 |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.889 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.10_2155) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 42.614 | 50.000 | 2.040 |
| High resolution limit [Å] | 1.954 | 4.240 | 1.970 |
| Rmerge | 0.114 | 0.076 | 0.329 |
| Rmeas | 0.125 | 0.082 | 0.436 |
| Rpim | 0.049 | 0.031 | 0.283 |
| Total number of observations | 179032 | ||
| Number of reflections | 33667 | ||
| <I/σ(I)> | 10.2 | ||
| Completeness [%] | 90.8 | 99.8 | 50.4 |
| Redundancy | 5.3 | 7 | 1.6 |
| CC(1/2) | 0.993 | 0.817 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 7.5 | 293 | Crystals grown in a reservoir solution of 23% PEG 8000 and 0.1M HEPES pH 7.5 and flash frozen in liquid nitrogen with 20% PEG 400 as a cryoprotectant |
