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38WT

Crystal structure of the CFTR inhibitory factor Cif with the L174A mutation

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsNSLS-II BEAMLINE 17-ID-1
Synchrotron siteNSLS-II
Beamline17-ID-1
Temperature [K]100
Detector technologyPIXEL
Collection date2025-03-14
DetectorDECTRIS EIGER X 9M
Wavelength(s)0.92019
Spacegroup nameC 1 2 1
Unit cell lengths168.707, 84.197, 89.526
Unit cell angles90.00, 100.34, 90.00
Refinement procedure
Resolution43.730 - 1.520
R-factor0.1576
Rwork0.157
R-free0.17360
Structure solution methodMOLECULAR REPLACEMENT
RMSD bond length0.006
RMSD bond angle0.860
Data reduction softwareXDS
Data scaling softwareXSCALE
Phasing softwarePHASER
Refinement softwarePHENIX (2.0_5936)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]43.7301.570
High resolution limit [Å]1.5201.520
Rmerge0.0510.614
Rmeas0.0580.717
Rpim0.0270.361
Number of reflections18660617976
<I/σ(I)>14.011.77
Completeness [%]98.795.57
Redundancy4.43.8
CC(1/2)0.9990.683
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP529115% (w/v) PEG 8000, 200 mM calcium chloride, 100 mM sodium acetate, pH 5.0

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