6SLU

Structure of the native full-length HIV-1 capsid protein A92E in helical assembly (-13,11)


ELECTRON MICROSCOPY

Refinement

RMS Deviations
KeyRefinement Restraint Deviation
f_dihedral_angle_d11.058
f_angle_d0.628
f_chiral_restr0.044
f_plane_restr0.004
f_bond_d0.003
Sample
In vitro assembled HIV-1 capsid in tubular assembly
Specimen Preparation
Sample Aggregation StateHELICAL ARRAY
Vitrification Instrument
Cryogen NameETHANE
Sample Vitrification Details
3D Reconstruction
Reconstruction MethodHELICAL
Number of Particles88436
Reported Resolution (Å)4.7
Resolution MethodFSC 0.143 CUT-OFF
Other Details
Refinement Type
Symmetry TypeHELICAL
Axial SymmetryC2
Axial Rise6.6
Angular Rotation165.3
Map-Model Fitting and Refinement
Id1
Refinement SpaceREAL
Refinement ProtocolFLEXIBLE FIT
Refinement TargetCross-correlation coefficient
Overall B Value72.14
Fitting Procedure
Details
Data Acquisition
Detector TypeGATAN K2 SUMMIT (4k x 4k)
Electron Dose (electrons/Å**2)40
Imaging Experiment1
Date of Experiment
Temperature (Kelvin)
Microscope ModelFEI POLARA 300
Minimum Defocus (nm)
Maximum Defocus (nm)
Minimum Tilt Angle (degrees)
Maximum Tilt Angle (degrees)
Nominal CS2
Imaging ModeBRIGHT FIELD
Specimen Holder ModelOTHER
Nominal Magnification
Calibrated Magnification
SourceFIELD EMISSION GUN
Acceleration Voltage (kV)300
Imaging Details
EM Software
TaskSoftware PackageVersion
PARTICLE SELECTIONRELION2.0;3.0
CTF CORRECTIONRELION2.0; 3.0
MODEL FITTINGCoot
INITIAL EULER ASSIGNMENTRELION2.0; 3.0
FINAL EULER ASSIGNMENTRELION2.0; 3.0
CLASSIFICATIONRELION2.0;3.0
RECONSTRUCTIONRELION2.0; 3.0
MODEL REFINEMENTPHENIX
Image Processing
CTF Correction TypeCTF Correction DetailsNumber of Particles SelectedParticle Selection Details
PHASE FLIPPING AND AMPLITUDE CORRECTION