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 method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SOLEIL BEAMLINE PROXIMA 2
Synchrotron site	SOLEIL
Beamline	PROXIMA 2
Temperature [K]	100
Detector technology	PIXEL
Collection date	2017-10-08
Detector	DECTRIS EIGER X 9M
Wavelength(s)	0.9801
Spacegroup name	P 1 21 1
Unit cell lengths	76.971, 108.260, 223.535
Unit cell angles	90.00, 93.22, 90.00

Refinement procedure

Resolution	49.050 - 2.989
Rwork	0.204
R-free	0.23950
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	7a59
RMSD bond length	0.004
RMSD bond angle	0.598
Data reduction software	XDS
Data scaling software	Aimless (0.5.32)
Phasing software	PHENIX
Refinement software	PHENIX (1.10.1_2155)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	49.600	49.600	3.050
High resolution limit [Å]	2.989	14.640	2.990
Rmerge	0.184	0.051	1.411
Rmeas	0.198	0.056	1.544
Rpim	0.075	0.023	0.616
Total number of observations		3739	24431
Number of reflections	73919	661	4043
<I/σ(I)>	7.8	26.1	1.2
Completeness [%]	99.3	96.8	89.2
Redundancy	7	5.7	6
CC(1/2)	0.995	0.997	0.555

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	291.15	0.5 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