6C0B
Structural basis for recognition of frizzled proteins by Clostridium difficile toxin B
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 24-ID-C |
Synchrotron site | APS |
Beamline | 24-ID-C |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2016-04-10 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 1 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 74.611, 175.613, 174.423 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 87.806 - 2.500 |
R-factor | 0.2006 |
Rwork | 0.199 |
R-free | 0.23740 |
Structure solution method | SAD |
RMSD bond length | 0.008 |
RMSD bond angle | 1.017 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | PHENIX |
Refinement software | PHENIX (1.11.1_2575) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 87.860 | 2.560 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.047 | 0.595 |
Number of reflections | 39399 | 3920 |
<I/σ(I)> | 18.25 | |
Completeness [%] | 98.0 | |
Redundancy | 3.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 292.15 | 0.1 M sodium acetate (pH 5.0) and 1 M ammonium sulfate |