The potential for Bayesian compressive sensing to significantly reduce electron dose in high-resolution STEM images

Microscopy ◽  
2013 ◽  
Vol 63 (1) ◽  
pp. 41-51 ◽  
Author(s):  
Andrew Stevens ◽  
Hao Yang ◽  
Lawrence Carin ◽  
Ilke Arslan ◽  
Nigel D. Browning
Keyword(s):  
High Resolution ◽  
Compressive Sensing ◽  
Electron Dose

Some problems and solutions in electron energy loss spectroscopy of cryosections

1993 ◽  
Vol 51 ◽  
pp. 566-567
Author(s):  
Zhifeng Shao ◽  
Ruoya Ho ◽  
Andrew P. Somlyo
Keyword(s):  
High Resolution ◽  
Energy Loss ◽  
Electron Energy ◽  
Electron Energy Loss Spectroscopy ◽  
Biological Research ◽  
Specimen Thickness ◽  
Elemental Distribution ◽  
Electron Dose ◽  
Simple Assumption ◽  
Electron Energy Loss

Electron energy loss spectroscopy (EELS) has been a powerful tool for high resolution studies of elemental distribution, as well as electronic structure, in thin samples. Its foundation for biological research has been laid out nearly two decades ago, and in the subsequent years it has been subjected to rigorous, but by no means extensive research. In particular, some problems unique to EELS of biological samples, have not been fully resolved. In this article we present a brief summary of recent methodological developments, related to biological applications of EELS, in our laboratory. The main purpose of this work was to maximize the signal to noise ratio (S/N) for trace elemental analysis at a minimum dose, in order to reduce the electron dose and/or time required for the acquisition of high resolution elemental maps of radiation sensitive biological materials.Based on the simple assumption of Poisson distribution of independently scattered electrons, it had been generally assumed that the optimum specimen thickness, at which the S/N is a maximum, must be the total inelastic mean free path of the beam electron in the sample.

scholarly journals High-Resolution Passive SAR Imaging Exploiting Structured Bayesian Compressive Sensing

2015 ◽  
Vol 9 (8) ◽  
pp. 1484-1497 ◽  
Author(s):  
Qisong Wu ◽  
Yimin D. Zhang ◽  
Moeness G. Amin ◽  
Braham Himed
Keyword(s):  
High Resolution ◽  
Compressive Sensing ◽  
Sar Imaging

Application of a slow-scan CCD camera in protein electron crystallography at 400 KV

1995 ◽  
Vol 53 ◽  
pp. 8-9
Author(s):  
Jaap Brink ◽  
Michael B. Sherman ◽  
Wah Chiu
Keyword(s):  
High Resolution ◽  
Fiber Optics ◽  
Electronic Device ◽  
Ccd Camera ◽  
Photographic Film ◽  
Electron Crystallography ◽  
Camera Model ◽  
Electron Dose ◽  
Voltage Electron ◽  
Diffraction Patterns

In protein electron crystallography, high resolution amplitudes and phases are required for a 3D reconstruction of a protein in which one can trace the Cα-backbone. Recording of these amplitudes and phases has so far been done on photographic film. In principle they can be obtained with higher fidelity using an electronic device, such as a slow-scan charge-coupled device (CCD) camera. We use a 1024 × 1024 Gatan CCD camera (model 679) attached to a JEOL 4000EX intermediate voltage electron cryo-microscope. The camera has a 20-30 μm thin P43 phosphor scintillator and an extra set of fiber optics, that reduces the number of x-ray pixels in acquired frames. In this abstract, we will focus on several issues related to the CCD camera in obtaining high resolution diffraction patterns and images from thin protein crystals.To obtain electron diffraction patterns with sufficient statistical definition, one needs to use an adequate electron dose. However, at exposures well above 0.25 e/Å2, the pattern will suffer from blooming due to the central beam.

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