@article{10889,
  abstract     = {Genetically encoded tags have introduced extensive lines of application from purification of tagged proteins to their visualization at the single molecular, cellular, histological and whole-body levels. Combined with other rapidly developing technologies such as clustered regularly interspaced palindromic repeats (CRISPR)/CRISPR-associated protein 9 (Cas9) system, proteomics, super-resolution microscopy and proximity labeling, a large variety of genetically encoded tags have been developed in the last two decades. In this review, I focus on the current status of tag development for electron microscopic (EM) visualization of proteins with metal particle labeling. Compared with conventional immunoelectron microscopy using gold particles, tag-mediated metal particle labeling has several advantages that could potentially improve the sensitivity, spatial and temporal resolution, and applicability to a wide range of proteins of interest (POIs). It may enable researchers to detect single molecules in situ, allowing the quantitative measurement of absolute numbers and exact localization patterns of POI in the ultrastructural context. Thus, genetically encoded tags for EM could revolutionize the field as green fluorescence protein did for light microscopy, although we still have many challenges to overcome before reaching this goal.},
  author       = {Shigemoto, Ryuichi},
  issn         = {2050-5701},
  journal      = {Microscopy},
  number       = {Supplement_1},
  pages        = {i72--i80},
  publisher    = {Oxford Academic},
  title        = {{Electron microscopic visualization of single molecules by tag-mediated metal particle labeling}},
  doi          = {10.1093/jmicro/dfab048},
  volume       = {71},
  year         = {2022},
}

@article{11648,
  abstract     = {Progress in structural membrane biology has been significantly accelerated by the ongoing 'Resolution Revolution' in cryo electron microscopy (cryo-EM). In particular, structure determination by single particle analysis has evolved into the most powerful method for atomic model building of multisubunit membrane protein complexes. This has created an ever increasing demand in cryo-EM machine time, which to satisfy is in need of new and affordable cryo electron microscopes. Here, we review our experience in using the JEOL CRYO ARM 200 prototype for the structure determination by single particle analysis of three different multisubunit membrane complexes: the Thermus thermophilus V-type ATPase VO complex, the Thermosynechococcus elongatus photosystem I monomer and the flagellar motor LP-ring from Salmonella enterica.},
  author       = {Gerle, Christoph and Kishikawa, Jun-ichi and Yamaguchi, Tomoko and Nakanishi, Atsuko and Çoruh, Mehmet Orkun and Makino, Fumiaki and Miyata, Tomoko and Kawamoto, Akihiro and Yokoyama, Ken and Namba, Keiichi and Kurisu, Genji and Kato, Takayuki},
  issn         = {2050-5701},
  journal      = {Microscopy},
  keywords     = {Radiology, Nuclear Medicine and imaging, Instrumentation, Structural Biology},
  number       = {5},
  pages        = {249--261},
  publisher    = {Oxford University Press},
  title        = {{Structures of multisubunit membrane complexes with the CRYO ARM 200}},
  doi          = {10.1093/jmicro/dfac037},
  volume       = {71},
  year         = {2022},
}