scholarly journals Dynamics of rebounding Bacillus subtilis spores determined using image-charge detection

2017 ◽  
Vol 43 (4) ◽  
pp. 481-492 ◽  
Author(s):  
Brandon L. Barney ◽  
Daniel E. Austin
2019 ◽  
Vol 52 (30) ◽  
pp. 305103 ◽  
Author(s):  
Paul Räcke ◽  
Robert Staacke ◽  
Jürgen W Gerlach ◽  
Jan Meijer ◽  
Daniel Spemann

2020 ◽  
Vol 91 (5) ◽  
pp. 053302
Author(s):  
Jace Rozsa ◽  
Yixin Song ◽  
Devon Webb ◽  
Naomi Debaene ◽  
Austin Kerr ◽  
...  

2011 ◽  
Vol 83 (3) ◽  
pp. 950-956 ◽  
Author(s):  
John W. Smith ◽  
Elizabeth E. Siegel ◽  
Joshua T. Maze ◽  
Martin F. Jarrold

2020 ◽  
Vol 31 (10) ◽  
pp. 2161-2170
Author(s):  
Elaura L. Gustafson ◽  
Halle V. Murray ◽  
Tabitha Caldwell ◽  
Daniel E. Austin

Author(s):  
Yimei Zhu ◽  
J. Tafto

The electron holes confined to the CuO2-plane are the charge carriers in high-temperature superconductors, and thus, the distribution of charge plays a key role in determining their superconducting properties. While it has been known for a long time that in principle, electron diffraction at low angles is very sensitive to charge transfer, we, for the first time, show that under a proper TEM imaging condition, it is possible to directly image charge in crystals with a large unit cell. We apply this new way of studying charge distribution to the technologically important Bi2Sr2Ca1Cu2O8+δ superconductors.Charged particles interact with the electrostatic potential, and thus, for small scattering angles, the incident particle sees a nuclei that is screened by the electron cloud. Hence, the scattering amplitude mainly is determined by the net charge of the ion. Comparing with the high Z neutral Bi atom, we note that the scattering amplitude of the hole or an electron is larger at small scattering angles. This is in stark contrast to the displacements which contribute negligibly to the electron diffraction pattern at small angles because of the short g-vectors.


Author(s):  
Dwight Anderson ◽  
Charlene Peterson ◽  
Gursaran Notani ◽  
Bernard Reilly

The protein product of cistron 3 of Bacillus subtilis bacteriophage Ø29 is essential for viral DNA synthesis and is covalently bound to the 5’-termini of the Ø29 DNA. When the DNA-protein complex is cleaved with a restriction endonuclease, the protein is bound to the two terminal fragments. The 28,000 dalton protein can be visualized by electron microscopy as a small dot and often is seen only when two ends are in apposition as in multimers or in glutaraldehyde-fixed aggregates. We sought to improve the visibility of these small proteins by use of antibody labeling.


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