ELECTRON MICROSCOPY

Sample

ABETA(1-42) AMYLOID-LIKE FIBRIL

Specimen Preperation
Sample Aggregation State FILAMENT
Vitrification Instrument GATAN CRYOPLUNGE 3
Cryogen Name ETHANE
Sample Vitrification Details 4 SEC BACKSIDE BLOTTING
3D Reconstruction
Reconstruction Method HELICAL
Number of Particles 62320
Reported Resolution (Å) 5
Resolution Method ?
Other Details FINAL MAP WAS CALCULATED FROM 29 SINGLE FILAMENT RECONSTRUCTIONS. DATA USED FOR REFINEMENT WAS NEVER BELOW 10 ANGSTROM RESOLUTION. RESOLUTION OF FIBRIL CORE IS ABOUT 5 ANGSTROM. 3 POSSIBLE MODELS FOR THE CENTRAL REGION OF A ABETA(1-42) FIBRIL RECONSTRUCTION. MODEL1 ABETA(17-42) MODEL2 ABETA( 16-41) MODEL3 ABETA(15-40) SUBMISSION BASED ON EXPERIMENTAL DATA FROM EMDB EMD-3132. (DEPOSITION ID: 13698).
Refinement Type
Symmetry Type HELICAL
Map-Model Fitting and Refinement
ID 1
Refinement Space REAL
Refinement Protocol OTHER
Refinement Target ELECTRON DENSITY
Overall B Value ?
Fitting Procedure ?
Details METHOD--DIREX REFINEMENT PROTOCOL--PEPTIDE CHAIN
Data Acquisition
Detector Type KODAK SO-163 FILM
Electron Dose (electrons/Å2) 30
Imaging Experiment
Date of Experiment 2010-02-05
Temprature (Kelvin)
Microscope Model FEI TECNAI F30
Minimum Defocus (nm) 1750
Maximum Defocus (nm) 3000
Minimum Tilt Angle (degrees) ?
Maximum Tilt Angle (degrees) ?
Nominal CS 2.0
Imaging Mode BRIGHT FIELD
Specimen Holder Model .
Nominal Magnification 59000
Calibrated Magnification 58333
Source FIELD EMISSION GUN
Acceleration Voltage (kV) 300
Imaging Details ?
Image Processing
CTF Correction Type CTF Correction Details Number of Particles Selected Particle Selection Details
? INDIVIDUAL HELICAL SUBUNITS
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