This page is intended to show examples of the MIDAS program. Feel free to submit a sample that you think would be a good illustration of deconvolution.
The AFM image of a sphere (shown as a contour map - see the scale on the right) gives an image of the tip when deconvoluted using the sphere. Here, the sphere is a 260 nm polystyrene typically used to calibrate other equipment. Note that the tip is triangular, and not the expected square pyramidal!
The original AFM image of the circular depressions (used for x-y calibration of the scanner) can be deconvoluted to give several images of the tip. Slight variations in the "tips" shown on the right are a reflection of the non-uniformity of the depressions in the left image.
The AFM image of a square depression (in this case a 200 mesh TEM grid) can be deconvoluted to give an image of the tip. Note that the scale on the left image is 120 microns and on the right its 5 microns (so alot of information in the image was not used!).
The following is a transcript of a segment of "Medical Breakthroughs" describing some of our previous research.
In the next few decades, it’s expected that the number of people 75 years of age or older will have increased by 200 percent. Diseases of aging will be one of the most pressing problems facing our health care system. Alzheimer’s is presently the fourth leading cause of death particularly for those over the age of 65.
Researchers still aren’t clear on how the disease progresses, but the discovery of a new imaging technique is bringing at least one thing into focus.
With the atomic force microscope we produce an image which is similar to a twisted ribbon in which there is a continuous flat structure which twists upon itself.
Michael Pollannen is describing the shape of protein filaments which assemble in the brain cells of Alzheimer’s victims. For decades, scientists have accepted a much different image of the filaments.
They found the protein to be forming two individual filaments that were wound together like a spiral staircase type model.
Peter Markiewicz explains how they got the clearer picture.
It’s essentially working like a record needle. Essentially, you’ve got a very sharp tip which passes over your sample.
Because the needle on the atomic force microscope is larger than the actual protein filament, a mathematical equation was worked out to compensate for the needle’s comparative largeness.
Getting a clear and accurate picture provides a clue as to how the filaments assemble. The twisted ribbon suggests that it forms in the same way as a crystal.
So these are the first steps in the attempt to develop techniques and agents that can stop the assembly of these filaments.
Last revised on 03-02-1999 by Peter Markiewicz