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6C0B

Structural basis for recognition of frizzled proteins by Clostridium difficile toxin B

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsAPS BEAMLINE 24-ID-C
Synchrotron siteAPS
Beamline24-ID-C
Temperature [K]100
Detector technologyPIXEL
Collection date2016-04-10
DetectorDECTRIS EIGER X 16M
Wavelength(s)1
Spacegroup nameC 2 2 21
Unit cell lengths74.611, 175.613, 174.423
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution87.806 - 2.500
R-factor0.2006
Rwork0.199
R-free0.23740
Structure solution methodSAD
RMSD bond length0.008
RMSD bond angle1.017
Data reduction softwareXDS
Data scaling softwareXDS
Phasing softwarePHENIX
Refinement softwarePHENIX (1.11.1_2575)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]87.8602.560
High resolution limit [Å]2.5002.500
Rmerge0.0470.595
Number of reflections393993920
<I/σ(I)>18.25
Completeness [%]98.0
Redundancy3.7
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP292.150.1 M sodium acetate (pH 5.0) and 1 M ammonium sulfate

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