4LSR
Crystal structure of broadly and potently neutralizing antibody VRC-CH31 in complex with HIV-1 clade A/E stran 93TH057 gp120 with LOOP D and Loop V5 from clade A strain KER_2018_11
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 22-BM |
Synchrotron site | APS |
Beamline | 22-BM |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2011-11-07 |
Detector | MARMOSAIC 225 mm CCD |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 64.934, 67.726, 220.120 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 39.500 - 2.280 |
R-factor | 0.198 |
Rwork | 0.194 |
R-free | 0.25800 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.005 |
RMSD bond angle | 0.854 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | PHENIX (dev_998) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.320 |
High resolution limit [Å] | 2.280 | 2.280 |
Rmerge | 0.134 | 0.602 |
Number of reflections | 41144 | |
<I/σ(I)> | 9.9 | |
Completeness [%] | 90.7 | 75 |
Redundancy | 5.1 | 3.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 8.5 | 293 | 0.1M Tris, 11% PEG 4000, 0.2 M Li2SO4, pH 8.5, temperature 293K |