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9FVI

Crystal structure of 14-3-3 sigma in complex with Tau pS214 peptide and covalent stabilizer JS18

This is a non-PDB format compatible entry.
Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE MASSIF-3
Synchrotron siteESRF
BeamlineMASSIF-3
Temperature [K]100
Detector technologyPIXEL
Collection date2023-07-12
DetectorDECTRIS EIGER X 4M
Wavelength(s)0.967697
Spacegroup nameC 2 2 21
Unit cell lengths82.161, 112.206, 62.350
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution45.460 - 1.550
R-factor0.18145
Rwork0.180
R-free0.21138
Structure solution methodMOLECULAR REPLACEMENT
RMSD bond length0.014
RMSD bond angle1.266
Data scaling softwareAimless
Phasing softwareMOLREP
Refinement softwareREFMAC (REFMAC5)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]62.3501.580
High resolution limit [Å]1.5501.550
Number of reflections420252045
<I/σ(I)>25.2
Completeness [%]99.8
Redundancy13.7
CC(1/2)0.9990.943
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, SITTING DROP27710mg/mL 14-3-3sigma delta C, 1.5eq peptide, 0.095 M HEPES pH 7.1, 28% PEG400, 0.19 M CaCl2, 5% (v/v) glycerol compound soaked

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