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Image Processing and Cryo-Transmission Electron Microscopy; Example of Human Proteasome

문지영|권오경|Seulgi Noh|최효선|전현범|노설지
한국현미경학회 (Korean Society Of Microscopy)|2018.03|Applied Microscopy|제48권 제1호|pp. 1-5|DOI 10.9729/AM.2018.48.1.1

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키워드

Negative stainingCryo-transmission electron microscopyProteasomeTwo-dimensional classification
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초록

Cryo-transmission electron microscopy (cryo-TEM) allows us to perform structural analysis of a analyses of large protein complexes, which are difficult to analyze using X-ray crystallography or nuclear magnetic resonance. The most common examples of proteins used are ribosomes and proteasomes. In this paper, we briefly describe the advantage of cryo-TEM and the process of two-dimensional classification by considering a human proteasome as an example.

Abstract

Cryo-transmission electron microscopy (cryo-TEM) allows us to perform structural analysis of a analyses of large protein complexes, which are difficult to analyze using X-ray crystallography or nuclear magnetic resonance. The most common examples of proteins used are ribosomes and proteasomes. In this paper, we briefly describe the advantage of cryo-TEM and the process of two-dimensional classification by considering a human proteasome as an example.

참고문헌 (22)

  1. Baker L A, "Radiation damage in electron cryomicroscopy", Methods Enzymol, 481, pp.371~388 (2010)
  2. Booth D S, "Visualizing proteins and macromolecular complexes by negative stain EM: from grid preparation to image acquisition", J. Vis. Exp., (58) (2011)[DOI]
  3. Brilot A F, "Beam-induced motion of vitrified specimen on holey carbon film", J. Struct. Biol., 177, pp.630~637 (2012)[DOI]
  4. Campbell M G, "Movies of ice-embedded particles enhance resolution in electron cryomicroscopy", Structure, 20, pp.1823~1828 (2012)[DOI]
  5. Cheng Y, "A primer to singleparticle cryo-electron microscopy", Cell, 161, pp.438~449 (2015)[DOI]
  6. Carlo S, "Cryonegative staining of macromolecular assemblies", Methods Enzymol, 481, pp.127~145 (2010)
  7. Dubochet J, "Cryo-EM--the first thirty years", J. Microsc., 245, pp.221~224 (2012)[DOI]
  8. Dubochet J, "Cryo-electron microscopy of vitrified specimens", Q. Rev. Biophys., 21, pp.129~228 (1988)[DOI]
  9. Dubochet J, "Vitrification of pure water for electron microscopy", J. Microsc., 124, pp.3~4 (1981)
  10. Frank J, "Averaging of low exposure electron micrographs of nonperiodic objects", Ultramicroscopy, 1, pp.159~162 (1975)[DOI]
  11. Frank J, "Computer averaging of electron micrographs of 40S ribosomal subunits", Science, 214, pp.1353~1355 (1981)[DOI]
  12. Grigorieff N, "FREALIGN: high-resolution refinement of single particle structures", J. Struct. Biol., 157, pp.117~125 (2007)[DOI]
  13. Henderson R, "Three-dimensional model of purple membrane obtained by electron microscopy", Nature, 257, pp.28~32 (1975)[DOI]
  14. Hohn M, "SPARX, a new environment for Cryo-EM image processing", J. Struct. Biol., 157, pp.47~55 (2007)[DOI]
  15. Luan B, "Structure of an endogenous yeast 26S proteasome reveals two major conformational states", Proc. Natl. Acad. Sci. U S A, 113, pp.2642~2647 (2016)[DOI]
  16. Merk A, "Breaking cryo-EM resolution barriers to facilitate drug discovery", Cell, 165, pp.1698~1707 (2016)[DOI]
  17. Nogales E, "Cryo-EM: a unique tool for the visualization of macromolecular complexity. Mol", Cell, 58, pp.677~689 (2015)
  18. Ohi M, "Negative staining and image classification--powerful tools in modern electron microscopy", Biol. Proced. Online, 6, pp.23~34 (2004)[DOI]
  19. Radermacher M, "Threedimensional reconstruction from a single-exposure, random conical tilt series applied to the 50S ribosomal subunit of Escherichia coli", J. Microsc., 146, pp.113~136 (1987)[DOI]
  20. Rames M, "Optimized negative staining: a highthroughput protocol for examining small and asymmetric protein structure by electron microscopy", J. Vis. Exp., (90), pp.e51087~ (2014)
  21. Scheres S H, "RELION: implementation of a Bayesian approach to cryo-EM structure determination", J. Struct. Biol., 180, pp.519~530 (2012)[DOI]
  22. Tang G, "EMAN2: an extensible image processing suite for electron microscopy", J. Struct. Biol., 157, pp.38~46 (2007)[DOI]

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