Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Sana Azim"'
Publikováno v:
Ultramicroscopy. 242:113611
MATLAB scripts were designed to compute the sample-limited spatial resolution in transmission electron microscopy (TEM) and scanning TEM (STEM) as a function of different microscopy parameters including the electron dose eD, sample geometry, and mate
Autor:
Eike C. Schulz, Sana Azim, Jan-Philipp Leimkohl, Michiel B. de Kock, Günther Kassier, Friedjof Tellkamp, Niels de Jonge, Ernesto Rafael Osorio-Blanco, Sercan Keskin, Marcelo Calderón, R. J. Dwayne Miller, Josef Gonschior, Lindsey A. Bultema, Robert Bücker
Publikováno v:
Microscopy and Microanalysis
Liquid-phase transmission electron microscopy is a technique for simultaneous imaging of the structure and dynamics of specimens in a liquid environment. The conventional sample geometry consists of a liquid layer tightly sandwiched between two Si3N4
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a904c6a189a5a6c8c9ac958fb382432a
https://hdl.handle.net/21.11116/0000-0008-0420-F21.11116/0000-0007-87FC-521.11116/0000-0007-87FF-2
https://hdl.handle.net/21.11116/0000-0008-0420-F21.11116/0000-0007-87FC-521.11116/0000-0007-87FF-2
Publikováno v:
The Journal of Chemical Physics
High energy electron scattering of liquid water (H2O) at near-ambient temperature and pressure was performed in a transmission electron microscope (TEM) to determine the radial distribution of water, which provides information on intra- and intermole
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::33fab34f345368d165c296eb3acae3ee
https://hdl.handle.net/21.11116/0000-0007-6FC4-021.11116/0000-0007-6FC6-E21.11116/0000-0007-6FC7-D
https://hdl.handle.net/21.11116/0000-0007-6FC4-021.11116/0000-0007-6FC6-E21.11116/0000-0007-6FC7-D
Autor:
Rachel W. Martin, R. J. Dwyane Miller, Kyle W. Roskamp, Günther Kassier, Brenna Norton-Baker, Sana Azim, Marc A. Sprague-Piercy
Publikováno v:
Biochemistry
Divalent metal cations can play a role in protein aggregation diseases, including cataract. Here we compare the aggregation of human γS-crystallin, a key structural protein of the eye lens, via mutagenesis, ultraviolet light damage, and the addition
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a6821f5630a2ecb2d6d6c76c363e9e92
https://hdl.handle.net/21.11116/0000-0006-A0A8-721.11116/0000-0006-A0AA-521.11116/0000-0006-A0AB-4
https://hdl.handle.net/21.11116/0000-0006-A0A8-721.11116/0000-0006-A0AA-521.11116/0000-0006-A0AB-4