R
Ralph Feder
Researcher at IBM
Publications - 50
Citations - 1367
Ralph Feder is an academic researcher from IBM. The author has contributed to research in topics: Microscopy & X-ray lithography. The author has an hindex of 20, co-authored 50 publications receiving 1345 citations. Previous affiliations of Ralph Feder include Imperial College London.
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Transmission microscopy of unmodified biological materials. Comparative radiation dosages with electrons and ultrasoft X-ray photons
TL;DR: Estimates of the maximum resolutions obtainable with electrons and photons, consistent with structural survival of the specimen, are obtained, as are data on optimal operating conditions for microscopy with the two particles.
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Potential Operating Region for Ultrasoft X-ray Microscopy of Biological Materials
TL;DR: Calculations are presented which indicate an extensive suboptical region in the microscopy of biological materials in their natural state which is accessible to ultrasoft x-ray transmission microscopy and radiation dosage levels to the specimen are lower than in electron microscopy.
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X-ray holograms at improved resolution: a study of zymogen granules.
M Howells,Chris Jacobsen,Janos Kirz,Ralph Feder,Kenneth R. McQuaid,Kenneth R. McQuaid,S. S. Rothman,S. S. Rothman +7 more
TL;DR: With a recently developed x-rays source based on an undulator on an electron storage ring, and high resolution x-ray resist, a hologram has been recorded at about 400-angstrom resolution, which is higher than that of the light microscope.
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High-resolution soft x-ray microscopy.
Ralph Feder,Eberhard Spiller,J. Topalian,Alec N. Broers,W Gudat,BJ Panessa,ZA Zadunaisky,J Sedat +7 more
TL;DR: A high-resolution scanning electron microscope with a short-focal-length final lens, operating in the "low-loss" mode, is used to make the smallest features in the x-ray replica visible.
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Direct imaging of live human platelets by flash x-ray microscopy.
TL;DR: A 100-nanosecond pulse of long-wavelength x-rays was used to produce high-resolution stop-motion images of living human platelets, and some aspects of the structure conform to those seen in dehydrated specimens, novel features are apparent.