8G8C
Crystal structure of DH1322.1 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 | 2022-10-22 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 1 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 75.308, 182.950, 84.414 |
Unit cell angles | 90.00, 92.28, 90.00 |
Refinement procedure
Resolution | 28.680 - 2.080 |
R-factor | 0.2002 |
Rwork | 0.199 |
R-free | 0.22850 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.013 |
RMSD bond angle | 1.166 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | PHENIX |
Refinement software | PHENIX (1.20) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 28.700 | 2.160 |
High resolution limit [Å] | 2.080 | 2.080 |
Rmerge | 0.044 | 0.320 |
Number of reflections | 65739 | 5860 |
<I/σ(I)> | 13 | |
Completeness [%] | 96.9 | |
Redundancy | 3.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 298 | 25% PEG 1500 and 0.1M SPG buffer pH 8.5 |