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7A5A

Crimean-Congo Hemorrhagic Fever Virus Envelope Glycoprotein Gc W1191H/W1197A/W1199A Mutant in Postfusion Conformation (Monoclinic Crystal Form)

This is a non-PDB format compatible entry.
Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsSOLEIL BEAMLINE PROXIMA 2
Synchrotron siteSOLEIL
BeamlinePROXIMA 2
Temperature [K]100
Detector technologyPIXEL
Collection date2017-10-08
DetectorDECTRIS EIGER X 9M
Wavelength(s)0.9801
Spacegroup nameP 1 21 1
Unit cell lengths76.971, 108.260, 223.535
Unit cell angles90.00, 93.22, 90.00
Refinement procedure
Resolution49.050 - 2.989
Rwork0.204
R-free0.23950
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)7a59
RMSD bond length0.004
RMSD bond angle0.598
Data reduction softwareXDS
Data scaling softwareAimless (0.5.32)
Phasing softwarePHENIX
Refinement softwarePHENIX (1.10.1_2155)
Data quality characteristics
 OverallInner shellOuter shell
Low resolution limit [Å]49.60049.6003.050
High resolution limit [Å]2.98914.6402.990
Rmerge0.1840.0511.411
Rmeas0.1980.0561.544
Rpim0.0750.0230.616
Total number of observations373924431
Number of reflections739196614043
<I/σ(I)>7.826.11.2
Completeness [%]99.396.889.2
Redundancy75.76
CC(1/2)0.9950.9970.555
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP7.5291.150.5 uL of 13.4 mg/mL protein in 20 mM Tris-Cl pH 8.0, 150 mM NaCl were added to 0.5 uL of reservoir solution containing 0.1 M HEPES pH 7.5, 10% (w/v) PEG 8K, 8% (v/v) ethylene glycol

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