@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},
}

@article{8447,
  abstract     = {Solid-state NMR spectroscopy can provide site-resolved information about protein dynamics over many time scales. Here we combine protein deuteration, fast magic-angle spinning (~45–60 kHz) and proton detection to study dynamics of ubiquitin in microcrystals, and in particular a mutant in a region that undergoes microsecond motions in a β-turn region in the wild-type protein. We use 15N R1ρ relaxation measurements as a function of the radio-frequency (RF) field strength, i.e. relaxation dispersion, to probe how the G53A mutation alters these dynamics. We report a population-inversion of conformational states: the conformation that in the wild-type protein is populated only sparsely becomes the predominant state. We furthermore explore the potential to use amide-1H R1ρ relaxation to obtain insight into dynamics. We show that while quantitative interpretation of 1H relaxation remains beyond reach under the experimental conditions, due to coherent contributions to decay, one may extract qualitative information about flexibility.},
  author       = {Gauto, Diego F. and Hessel, Audrey and Rovó, Petra and Kurauskas, Vilius and Linser, Rasmus and Schanda, Paul},
  issn         = {0926-2040},
  journal      = {Solid State Nuclear Magnetic Resonance},
  keywords     = {Nuclear and High Energy Physics, Instrumentation, General Chemistry, Radiation},
  number       = {10},
  pages        = {86--95},
  publisher    = {Elsevier},
  title        = {{Protein conformational dynamics studied by 15N and 1HR1ρ relaxation dispersion: Application to wild-type and G53A ubiquitin crystals}},
  doi          = {10.1016/j.ssnmr.2017.04.002},
  volume       = {87},
  year         = {2017},
}