3I50
Crystal structure of the West Nile Virus envelope glycoprotein in complex with the E53 antibody Fab
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 4.2.2 |
Synchrotron site | ALS |
Beamline | 4.2.2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-06-06 |
Detector | NOIR-1 |
Wavelength(s) | 1.240 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 146.410, 160.140, 43.880 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 3.000 |
Rwork | 0.247 |
R-free | 0.34400 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.004 |
RMSD bond angle | 0.858 |
Data reduction software | d*TREK |
Data scaling software | d*TREK (9.4D) |
Phasing software | PHASER |
Refinement software | PHENIX |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.150 | 3.110 |
High resolution limit [Å] | 3.000 | 3.000 |
Rmerge | 0.053 | 0.453 |
Number of reflections | 21428 | |
<I/σ(I)> | 12.1 | 2 |
Completeness [%] | 99.5 | 99.8 |
Redundancy | 4.45 | 4.39 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | 30% PEG 300, 0.1 M MES, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |