8G8D
Crystal structure of DH1346 Fab in complex with HIV proximal MPER peptide
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 | PIXEL |
Collection date | 2022-11-22 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 1 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 41.069, 115.513, 231.322 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 37.980 - 2.020 |
R-factor | 0.2005 |
Rwork | 0.198 |
R-free | 0.23350 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.005 |
RMSD bond angle | 0.723 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHENIX |
Refinement software | PHENIX (1.20) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 37.980 | 2.100 |
High resolution limit [Å] | 2.020 | 2.020 |
Rmerge | 0.075 | 0.530 |
Number of reflections | 67030 | 5929 |
<I/σ(I)> | 12.1 | |
Completeness [%] | 91.7 | |
Redundancy | 3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 4.5 | 298 | 25% PEG 1500, 0.1M Sodium acetate/acetic acid pH4.5, 30% MPD, and 30% dextran sulfate sodium salt |