5EII
Structural determination of an protein complex of a Fab with increased solubility
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 23-ID-B |
Synchrotron site | APS |
Beamline | 23-ID-B |
Temperature [K] | 80 |
Detector technology | IMAGE PLATE |
Collection date | 2013-12-13 |
Detector | MAR scanner 300 mm plate |
Wavelength(s) | 0.987 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 81.486, 62.945, 161.828 |
Unit cell angles | 90.00, 94.00, 90.00 |
Refinement procedure
Resolution | 46.384 - 2.440 |
R-factor | 0.1875 |
Rwork | 0.185 |
R-free | 0.23260 |
RMSD bond length | 0.004 |
RMSD bond angle | 0.716 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | MOLREP |
Refinement software | PHENIX ((1.10_2152: ???)) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 46.384 |
High resolution limit [Å] | 2.437 |
Number of reflections | 61283 |
<I/σ(I)> | 12.1 |
Completeness [%] | 99.4 |
Redundancy | 3.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | LIQUID DIFFUSION | 293 | Crystals were grown by hanging drop liquid diffusion by adding a solution containing 20% PEG 3350 and Sodium Acetate, pH 5.5 |