Toward High-Resolution Cryo-Electron Microscopy: Technical Review on Microcrystal-Electron Diffraction
2
조회
0
다운로드
0
인용
0
참고문헌
키워드
초록
Cryo-electron microscopy (cryo-EM) is arguably the most powerful tool used in structural biology. It is an important analytical technique that is used for gaining insight into the functional and molecular mechanisms of biomolecules involved in several physiological processes. Cryo-EM can be separated into the following three groups according to the analytical purposes and the features of the biological samples: cryo-electron tomography (cryo-ET), cryo-single-particle reconstruction, and cryo-electron crystallography. Cryotomography is a unique EM technique that is used to study intact biomolecular complexes within their original environments; it can provide mechanistic insights that are challenging for other EM-methods. However, the resolution of reconstructed three-dimensional (3D) models generated by cryo-ET is relatively low, while single-particle reconstruction can reproduce biomolecular structures having near-atomic resolution without the need for crystallization unless the samples are large (>200 kDa) and highly symmetrical. Cryoelectron crystallography is subdivided into the following two categories according to the types of samples: one category that deals with two-dimensional (2D) crystalline arrays and the other category that uses 3D crystals. These two categories of electron-crystallographic techniques use different diffraction data obtained from still diffraction and continuousrotation diffraction. In this paper, we review crystal-based cryo-EM techniques and focus on the recently developed 3D electron-crystallographic technique called microcrystalelectron diffraction.
Abstract
Cryo-electron microscopy (cryo-EM) is arguably the most powerful tool used in structural biology. It is an important analytical technique that is used for gaining insight into the functional and molecular mechanisms of biomolecules involved in several physiological processes. Cryo-EM can be separated into the following three groups according to the analytical purposes and the features of the biological samples: cryo-electron tomography (cryo-ET), cryo-single-particle reconstruction, and cryo-electron crystallography. Cryotomography is a unique EM technique that is used to study intact biomolecular complexes within their original environments; it can provide mechanistic insights that are challenging for other EM-methods. However, the resolution of reconstructed three-dimensional (3D) models generated by cryo-ET is relatively low, while single-particle reconstruction can reproduce biomolecular structures having near-atomic resolution without the need for crystallization unless the samples are large (>200 kDa) and highly symmetrical. Cryoelectron crystallography is subdivided into the following two categories according to the types of samples: one category that deals with two-dimensional (2D) crystalline arrays and the other category that uses 3D crystals. These two categories of electron-crystallographic techniques use different diffraction data obtained from still diffraction and continuousrotation diffraction. In this paper, we review crystal-based cryo-EM techniques and focus on the recently developed 3D electron-crystallographic technique called microcrystalelectron diffraction.
참고문헌 (22)
- Asano S, "In situ cryo-electron tomography: A post-reductionist approach to structural biology", J. Mol. Biol, 428, pp.332~343 (2016)
- Bendersky L A, "Electron diffraction using transmission electron microscopy", J. Res. Natl. Inst. Stand. Technol, 106, pp.997~1012 (2001)
- 정정민, "Recent Advances in Electron Crystallography", 한국현미경학회지, 47(3), pp.160~164 (2017), 한국현미경학회
- Dubochet J, "Cryo-EM—the first thirty years", J. Microsc, 245, pp.221~224 (2012)
- Frank J, "Single-particle reconstruction of biological macromolecules in electron microscopy—30 years", Q. Rev. Biophys, 42, pp.139~158 (2009)
- Frank J, "Generalized single-particle cryo-EM—a historical perspective", Microscopy (Oxf), 65, pp.3~8 (2016)
- Glaeser R M, "Limitations to significant information in biological electron microscopy as a result of radiation damage", J. Ultrastruct. Res, 36, pp.466~482 (1971)
- Gonen T, "Lipid-protein interactions in double-layered two-dimensional AQP0 crystals", Nature, 438, pp.633~638 (2005)
- Henderson R, "Realizing the potential of electron cryo-microscopy", Q. Rev. Biophys, 37, pp.3~13 (2004)
- Hyun J K, "Membrane remodeling by the double-barrel scaffolding protein of poxvirus", PLoS Pathog, 7, pp.e1002239~ (2011)
- Kimura Y, "Surface of bacteriorhodopsin revealed by high-resolution electron crystallography", Nature, 389, pp.206~211 (1997)
- Nannenga B L, "Protein structure determination by MicroED", Curr. Opin. Struct. Biol, 27, pp.24~31 (2014)
- Nannenga B L, "MicroED opens a new era for biological structure determination", Curr. Opin. Struct. Biol, 40, pp.128~135 (2016)
- Nannenga B L, "Structure of catalase determined by MicroED", Elife, 3, pp.e03600~ (2014)
- Nannenga B L, "High-resolution structure determination by continuous-rotation data collection in MicroED", Nat. Methods, 11, pp.927~930 (2014)
- Rodriguez J A, "Structure of the toxic core of alpha-synuclein from invisible crystals", Nature, 525, pp.486~490 (2015)
- Scherer S, "Single particle 3D reconstruction for 2D crystal images of membrane proteins", J. Struct. Biol, 185, pp.267~277 (2014)
- Shi D, "The collection of MicroED data for macromolecular crystallography", Nat. Protoc, 11, pp.895~904 (2016)
- Shi D, "Threedimensional electron crystallography of protein microcrystals", Elife, 2, pp.e01345~ (2013)
- Unwin N, "Structure and action of the nicotinic acetylcholine receptor explored by electron microscopy", FEBS Lett, 555, pp.91~95 (2003)
- Unwin P N, "Molecular structure determination by electron microscopy of unstained crystalline specimens", J. Mol. Biol, 94, pp.425~440 (1975)
- Yonekura K, "Electron crystallography of ultrathin 3D protein crystals: atomic model with charges", Proc. Natl. Acad. Sci. USA, 112, pp.3368~3373 (2015)