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9F2H

Crystal structure of SARS-CoV-2 N-protein C-terminal domain in complex with riluzole

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE ID23-1
Synchrotron siteESRF
BeamlineID23-1
Temperature [K]100
Detector technologyPIXEL
Collection date2021-07-10
DetectorDECTRIS EIGER2 X CdTe 16M
Wavelength(s)0.774899
Spacegroup nameI 1 2 1
Unit cell lengths93.056, 43.383, 109.326
Unit cell angles90.00, 91.44, 90.00
Refinement procedure
Resolution46.560 - 1.300
R-factor0.16856
Rwork0.168
R-free0.18898
Structure solution methodMOLECULAR REPLACEMENT
RMSD bond length0.006
RMSD bond angle1.360
Data reduction softwareXDS
Data scaling softwareXDS
Phasing softwareMOLREP
Refinement softwareREFMAC (5.8.0411)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]46.5601.320
High resolution limit [Å]1.3001.300
Rpim0.0260.363
Number of reflections1036024726
<I/σ(I)>12.31.9
Completeness [%]97.089.9
Redundancy5.54.7
CC(1/2)0.9990.685
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, SITTING DROP8.5291PEG 3350 38%, 0.1 M Tris pH 8.5, 50 mM ammonium sulfate and 1 mM InsP6. Protein:precipitant ratio 1:1. Protein concentration: 16.5 mg/ml. Protein buffer: 20 mM Tris pH 8.0 and 150 mM NaCl. Soaking o/n with saturated concentration of riluzole in PEG 3350 40%, 0.1 M Tris pH 8.5, 50 mM ammonium sulfate, 1 mM InsP6 condition.

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