5EWI
Crystal Structure of the Human Fab VRC38.01, an HIV-1 V1V2-Directed Neutralizing Antibody Isolated from Donor N90
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 | 2015-02-08 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 21 2 21 |
| Unit cell lengths | 62.353, 84.775, 90.003 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 31.176 - 1.600 |
| R-factor | 0.174 |
| Rwork | 0.173 |
| R-free | 0.20240 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4xmk |
| RMSD bond length | 0.008 |
| RMSD bond angle | 0.963 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.640 |
| High resolution limit [Å] | 1.600 | 3.950 | 1.600 |
| Rmerge | 0.083 | 0.048 | 0.636 |
| Rmeas | 0.090 | 0.053 | 0.693 |
| Rpim | 0.036 | 0.022 | 0.272 |
| Total number of observations | 403502 | ||
| Number of reflections | 63192 | ||
| <I/σ(I)> | 13.5 | ||
| Completeness [%] | 99.3 | 95.7 | 98.9 |
| Redundancy | 6.4 | 5.9 | 6.3 |
| CC(1/2) | 0.996 | 0.845 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 293 | 14% PEG400, 13% PEG8000, 0.1M Tris pH 8.5, 0.1M MgCl, No Cryo |
