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Electron Microscopy for Hydrophilic Specimen and Related Measurements

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Biochemistry".

Deadline for manuscript submissions: closed (30 September 2022) | Viewed by 1973

Special Issue Editor


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Guest Editor
Health and Medical Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), Central 6, 1-1-1 Higashi, Tsukuba, Ibaraki 305-8566, Japan
Interests: electron microscopy; liquid-phase EM; cryo-EM, molecular complex; biophysics; neural network; nanostructure
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Special Issue Information

Dear Colleagues,

High-resolution observation of biological specimens and material phenomena in hydrophilic conditions is a fascinating field that has a huge frontier. Recent advances in liquid-phase electron microscopy (EM) and cryo-EM have realized the observation of wet samples by electron microscopy, delivering significant findings in many research fields. In this Special Issue, we aim to include results from biological fields and material sciences and to consider the future direction of electron microscopy of hydrophilic specimens and its correlative microscopy. Observations of biological and medical samples, the nano-structures of materials and their dynamics are of high interest for this Special Issue. We also aim to address experimental and technical challenges that have to be met in order to realize a correlative measurement of the target molecules in a liquid. We envisage reports of novel specimen preparation methods, immuno-labeling techniques to realize visualization of molecules and data interpretation of results using informatics including artificial intelligence. We also welcome the development of new specimen holders that include a micro-fluidics chamber and of electro-chemical holders that allow phenomena to be clarified at a molecular level, and, of course, the modification of transmission EM (TEM), scanning EM (SEM) and scanning transmission EM (STEM) for their use. Studies of metal sedimentation and electro-chemical reactions are also of high interest for this Special Issue. Contributions relevant to basic biology, applied biology and diagnostic research are encouraged. Partial clinical research and survey studies are not within the focus of this Special Issue.

Dr. Chikara Sato
Guest Editor

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Keywords

  • environmental cell
  • cryo-electron microscopy
  • immuno-electron microscopy
  • cell signaling
  • comparative anatomy
  • diagnosis
  • molecular recognition
  • molecular complexes
  • electro-chemistry
  • metal sedimentation

Published Papers (1 paper)

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Research

17 pages, 7335 KiB  
Article
Elongation and Contraction of Scallop Sarcoplasmic Reticulum (SR): ATP Stabilizes Ca2+-ATPase Crystalline Array Elongation of SR Vesicles
by Jun Nakamura, Yuusuke Maruyama, Genichi Tajima, Makiko Suwa and Chikara Sato
Int. J. Mol. Sci. 2022, 23(6), 3311; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms23063311 - 18 Mar 2022
Cited by 1 | Viewed by 1582
Abstract
The Ca2+-ATPase is an integral transmembrane Ca2+ pump of the sarcoplasmic reticulum (SR). Crystallization of the cytoplasmic surface ATPase molecules of isolated scallop SR vesicles was studied at various calcium concentrations by negative stain electron microscopy. In the absence of [...] Read more.
The Ca2+-ATPase is an integral transmembrane Ca2+ pump of the sarcoplasmic reticulum (SR). Crystallization of the cytoplasmic surface ATPase molecules of isolated scallop SR vesicles was studied at various calcium concentrations by negative stain electron microscopy. In the absence of ATP, round SR vesicles displaying an assembly of small crystalline patches of ATPase molecules were observed at 18 µM [Ca2+]. These partly transformed into tightly elongated vesicles containing ATPase crystalline arrays at low [Ca2+] (≤1.3 µM). The arrays were classified as ‘’tetramer’’, “two-rail” (like a railroad) and ‘’monomer’’. Their crystallinity was low, and they were unstable. In the presence of ATP (5 mM) at a low [Ca2+] of ~0.002 µM, “two-rail” arrays of high crystallinity appeared more frequently in the tightly elongated vesicles and the distinct tetramer arrays disappeared. During prolonged (~2.5 h) incubation, ATP was consumed and tetramer arrays reappeared. A specific ATPase inhibitor, thapsigargin, prevented both crystal formation and vesicle elongation in the presence of ATP. Together with the second part of this study, these data suggest that the ATPase forms tetramer units and longer tetramer crystalline arrays to elongate SR vesicles, and that the arrays transform into more stable “two-rail” forms in the presence of ATP at low [Ca2+]. Full article
(This article belongs to the Special Issue Electron Microscopy for Hydrophilic Specimen and Related Measurements)
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