Yonekura K, Maki-Yonekura S (2016) Refinement of cryo-EM structures using scattering factors of charged atoms. Yonekura K, Kato K, Ogasawara M, Tomita M, Toyoshima C (2015) Electron crystallography of ultra-thin 3D protein crystals: atomic model with charges. Yonekura K, Braunfeld MB, Maki-Yonekura S, Agard DA (2006) Electron energy filtering significantly improves amplitude contrast of frozen-hydrated protein at 300 kV. Yonekura K, Maki-Yonekura S, Namba K (2002) Quantitative comparison of zero-loss and conventional electron diffraction from 2D and thin 3D protein crystals. Van Genderen E, Clabbers MTB, Das PP, Stewart A, Nederlof I, Barentsen KC, Portillo Q, Pannu NS, Nicolopoulos S, Gruene T, Abrahams JP (2016) Ab initio structure determination of nanocrystals of organic pharmaceutical compounds by electron diffraction at room temperature using a Timepix quantum area direct electron detector. Tegunov D, Xue L, Dienemann C, Cramer P, Mahamid J (2021) Multi-particle cryo-EM refinement with M visualizesribosome-antibiotic complex at 3.7 Å inside cells. Takaba K, Maki-Yonekura S, Yonekura K (2020) Collecting large datasets of rotational electron diffraction with ParallEM and SerialEM. Nannenga BL, Shi D, Leslie AGW, Gonen T (2014) High-resolution structure determination by continuous-rotation data collection in MicroED. Naitow H, Hamaguchi T, Maki-Yonekura S, Isogai M, Yoshikawa N, Yonekura K (2020) Apple latent spherical virus structure with stable capsid frame supports quasi-stable protrusions expediting genome release. Mastronarde DN (2005) Automated electron microscope tomography using robust prediction of specimen movements. Refinements of the CRYO ARM 300 System in RIKEN SPring-8 Center. Maki-Yonekura S, Hamaguchi T, Naitow H, Takaba K, Yonekura K (2021) Advances in Cryo-EM and ED with a cold-field emission beam and energy filtration. Kato K, Takaba K, Maki-Yonekura S, Mitoma N, Nakanishi Y, Nishihara T, Hatakeyama T, Kawada T, Hijikata Y, Pirillo J, Scott LT, Yonekura K, Segawa Y, Itami K (2021) Double-helix supramolecular nanofibers assembled from negatively curved nanographenes. Hamaguchi T, Kawakami K, Shinzawa-Itoh K, Inoue-Kashino N, Itoh S, Ifuku K, Yamashita E, Maeda K, Yonekura K, Kashino Y (2021) Structure of the far-red light utilizing photosystem I of Acaryochloris. Hamaguchi T, Maki-Yonekura S, Naitow H, Matsuura Y, Ishikawa T, Yonekura K (2019) A new cryo-EM system for single particle analysis. Electron 3D crystallography (3D ED/MicroED)Īngert I, Burmester C, Dinges C, Rose H, Schröder RR (1996) Elastic and inelastic scattering cross sections of amorphous layers of carbon and vitrified ice.This review introduces our recent results, progress, and perspective for running such cryo-EM system. Automated data collection allows high-throughput structure determination in both applications. For 3D electron crystallography, we are also routinely able to obtain highest-quality diffraction data thanks to higher-energy electrons and energy filtration. For single particle analysis, we are routinely able to reconstruct higher-resolution structures with better estimated B-factors for map sharpening from smaller numbers of images than can be obtained with conventional Schottky emission. The microscope has provided high quality data in both imaging and diffraction since July 2018. We designed such system and installed a JEOL CRYO ARM 300 electron microscope- the first machine of this model. A cryo-electron microscopy (cryo-EM) system equipped with a cold-field emission gun and an energy filter is well-suited for higher-resolution single particle analysis and high-precision 3D electron crystallography.
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