5KG9
Crystal structure of the gp120 v2 antibody RE505-22 Fab from IGH- and IGK-humanized mouse
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 93 |
| Detector technology | CCD |
| Collection date | 2015-06-09 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 72.183, 76.749, 184.287 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 39.507 - 2.300 |
| R-factor | 0.2418 |
| Rwork | 0.240 |
| R-free | 0.28070 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4hpy 3ffd |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.753 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.8.4_1496) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 39.507 | 2.340 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Rmerge | 0.110 | 0.570 |
| Number of reflections | 46019 | |
| <I/σ(I)> | 17.9 | 2.3 |
| Completeness [%] | 99.7 | 98.8 |
| Redundancy | 5.7 | 4.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | 0.2 M NaF, 20% PEG 3350 |
