ELECTRON MICROSCOPY
Sample |
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Procapsid of the bacteriophage alpha3 |
Specimen Preparation | |
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Sample Aggregation State | PARTICLE |
3D Reconstruction | |
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Reconstruction Method | SINGLE PARTICLE |
Number of Particles | 2378 |
Reported Resolution (Å) | 16 |
Resolution Method | |
Other Details | 2378 particles were included in the final reconstruction. The effective resolution is 15.0-16.0A. Higher resolution was not possible because of the ... |
Refinement Type | |
Symmetry Type | POINT |
Point Symmetry | I |
Map-Model Fitting and Refinement | |||||
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Id | 1 (1M06, 1CD3) | ||||
Refinement Space | REAL | ||||
Refinement Protocol | RIGID BODY FIT | ||||
Refinement Target | Best fit criterion used by the program EMfit is based on the average value of the density at all atomic sites in the fitted protein, the lack of atoms in negative density, and the absence of symmetry related atomic clashes. | ||||
Overall B Value | |||||
Fitting Procedure | |||||
Details | METHOD--General search followed by a climb procedure REFINEMENT PROTOCOL--rigid molecule fit using the program EMfit |
Data Acquisition | |||||||||
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Detector Type | KODAK SO-163 FILM | ||||||||
Electron Dose (electrons/Å**2) | 0.017 |
Imaging Experiment | 1 |
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Date of Experiment | 1998-10-16 |
Temperature (Kelvin) | 88 |
Microscope Model | FEI/PHILIPS CM200FEG/ST |
Minimum Defocus (nm) | 3200 |
Maximum Defocus (nm) | 1600 |
Minimum Tilt Angle (degrees) | |
Maximum Tilt Angle (degrees) | |
Nominal CS | 2 |
Imaging Mode | BRIGHT FIELD |
Specimen Holder Model | |
Nominal Magnification | 38000 |
Calibrated Magnification | 40000 |
Source | FIELD EMISSION GUN |
Acceleration Voltage (kV) | 200 |
Imaging Details |
EM Software | ||
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Task | Software Package | Version |
MODEL FITTING | EMfit | |
PARTICLE SELECTION | RobEM | |
RECONSTRUCTION | EM3DR |
Image Processing | ||||
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CTF Correction Type | CTF Correction Details | Number of Particles Selected | Particle Selection Details | |
CTF correction was done for each particle. |