3IXT
Crystal Structure of Motavizumab Fab Bound to Peptide Epitope
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 | CCD |
Collection date | 2009-04-04 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.82656 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 90.752, 90.752, 232.057 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 33.256 - 2.750 |
R-factor | 0.2162 |
Rwork | 0.213 |
R-free | 0.27400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2hwz |
RMSD bond length | 0.004 |
RMSD bond angle | 0.742 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | PHENIX ((phenix.refine)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.850 |
High resolution limit [Å] | 2.750 | 2.750 |
Number of reflections | 23510 | |
Completeness [%] | 93.5 | 88.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | 17.5% PEG 8000, 0.2 M zinc acetate, 0.1 M cacodylate pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |