1ZTX
West Nile Virus Envelope Protein DIII in complex with neutralizing E16 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 | 2004-08-05 |
Detector | BRUKER PROTEUM |
Wavelength(s) | 1.55 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 52.400, 83.300, 110.600 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.000 - 2.500 |
R-factor | 0.226 |
Rwork | 0.208 |
R-free | 0.28200 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | PDB ENTRIES 1S6N 2igf |
RMSD bond length | 0.007 |
RMSD bond angle | 1.500 |
Data scaling software | d*TREK (9.2LDz) |
Phasing software | MOLREP |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 47.320 | 2.590 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.083 | 0.306 |
Number of reflections | 16985 | |
<I/σ(I)> | 11.3 | 2.7 |
Completeness [%] | 97.6 | 82.7 |
Redundancy | 3.53 | 1.99 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 293 | PEG 4000, Glycine, Hepes, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |