4MWF
Structure of Hepatitis C Virus Envelope Glycoprotein E2 core bound to broadly neutralizing antibody AR3C
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL12-2 |
Synchrotron site | SSRL |
Beamline | BL12-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2013-01-19 |
Detector | MARMOSAIC 325 mm CCD |
Wavelength(s) | 1.033 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 47.132, 166.553, 209.963 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 49.078 - 2.645 |
R-factor | 0.2333 |
Rwork | 0.231 |
R-free | 0.27020 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.007 |
RMSD bond angle | 1.275 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | PHENIX ((phenix.refine: 1.8.2_1309)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 49.090 | 2.700 |
High resolution limit [Å] | 2.650 | 2.650 |
Number of reflections | 46174 | |
Completeness [%] | 93.4 | 76.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | 20% (w/v) PEG 4000, 10% (v/v) isopropanol, and 0.1 M HEPES pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |