8A1E

Rabies virus glycoprotein in complex with Fab fragments of 17C7 and 1112-1 neutralizing antibodies


ELECTRON MICROSCOPY

Refinement

RMS Deviations
KeyRefinement Restraint Deviation
f_dihedral_angle_d4.7288
f_angle_d0.523
f_chiral_restr0.0417
f_plane_restr0.0039
f_bond_d0.0031
Sample
Rabies virus glycoprotein (chain A) in complex with Fab 1112-1 (chains B and C) and Fab 17C7 (chains D and E)
Specimen Preparation
Sample Aggregation StatePARTICLE
Vitrification InstrumentFEI VITROBOT MARK IV
Cryogen NameETHANE
Sample Vitrification DetailsBlot for 3.5 seconds at -15 N blot force before plunging.
3D Reconstruction
Reconstruction MethodSINGLE PARTICLE
Number of Particles458014
Reported Resolution (Å)2.83
Resolution MethodFSC 0.143 CUT-OFF
Other DetailscryoSPARC non-uniform refinement was used.
Refinement Type
Symmetry TypePOINT
Point SymmetryC3
Map-Model Fitting and Refinement
Id1
Refinement SpaceREAL
Refinement ProtocolRIGID BODY FIT
Refinement Target
Overall B Value108
Fitting Procedure
DetailsModel building was performed with Coot and refined with Phenix.
Data Acquisition
Detector TypeGATAN K3 BIOQUANTUM (6k x 4k)
Electron Dose (electrons/Å**2)44.4
Imaging Experiment1
Date of Experiment
Temperature (Kelvin)
Microscope ModelFEI TITAN KRIOS
Minimum Defocus (nm)800
Maximum Defocus (nm)2600
Minimum Tilt Angle (degrees)
Maximum Tilt Angle (degrees)
Nominal CS2.7
Imaging ModeBRIGHT FIELD
Specimen Holder ModelFEI TITAN KRIOS AUTOGRID HOLDER
Nominal Magnification81000
Calibrated Magnification
SourceFIELD EMISSION GUN
Acceleration Voltage (kV)300
Imaging Details
EM Software
TaskSoftware PackageVersion
PARTICLE SELECTIONcryoSPARC3.1
IMAGE ACQUISITIONSerialEM
CTF CORRECTIONGctf1.06
MODEL FITTINGUCSF Chimera
INITIAL EULER ASSIGNMENTcryoSPARC3.1
FINAL EULER ASSIGNMENTcryoSPARC3.1
RECONSTRUCTIONcryoSPARC3.1
MODEL REFINEMENTPHENIX1.19.2_4158
Image Processing
CTF Correction TypeCTF Correction DetailsNumber of Particles SelectedParticle Selection Details
PHASE FLIPPING AND AMPLITUDE CORRECTION3112037Particles were automatically picked using circular blobs with a diameter of 80-150 Angstrom on cryoSPARC.