Tìm kiếm theo: Chủ đề Cryo-EM

Duyệt theo: 0-9 A B C D E F G H I J K L M N O P Q R S T U V W X Y Z
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  • OER000000810.pdf.jpg
  • Journal article


  • Tác giả : McSweeney, Donal M; McSweeney, Sean M; Liu, Qun (2020)

  • High-resolution single-particle cryo-EM data analysis relies on accurate particle picking. To facilitate the particle picking process, we have developed a self-supervised workflow. Our workflow includes an iterative strategy to use the 2D class average to improve training particles and a progressively improved convolutional neural network (CNN) for particle picking. To automate the selection of particles, we define a threshold (%/Res) using the ratio of percentage...

  • OER000002634.pdf.jpg
  • Journal article


  • Tác giả : Richards, Logan S. (2023)

  • Amyloid diseases are linked to the formation and persistence of large, multimeric structures in various tissues. Amyloid fibrils are characterized by a cross-beta scaffold in which identical protein molecules mate tightly as beta-strands to form a long, unbranched fibril1,2. Before amyloid-forming proteins assemble into fibrils, they can display a globular fold, requiring partial or total unfolding to convert into an amyloid state3,4. Debilitating ne...

  • OER000002758.pdf.jpg
  • Journal article


  • Tác giả : Kishikawa, Jun-ichi (2023)

  • The Na+-pumping NADH-ubiquinone oxidoreductase (Na+-NQR) couples electron transfer 3 from NADH to ubiquinone with Na+-pumping, generating an electrochemical Na+ gradient that 4 is essential for energy-consuming reactions in bacteria. Since Na+-NQR is exclusively found in 5 prokaryotes, it is a promising target for highly selective antibiotics. However, the molecular 6 mechanism of inhibition is not well-understood for lack of the atomic structural informa...

  • OER000002513.pdf.jpg
  • Journal article


  • Tác giả : Harder, Oliver F.  (2023)

  • Observing proteins as they perform their tasks has largely remained elusive, which has left our understanding of protein function fundamentally incomplete. To enable such observations, we have recently proposed a novel technique that improves the time resolution of cryo-electron microscopy (cryo EM) to microseconds. Here, we demonstrate that microsecond time-resolved cryo-EM enables observations of fast protein dynamics. We use our approach to elucidate&#...