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초록· 키워드
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Recent cryo-electron microscopy (EM) studies reported the structure of various types of proteins at high resolution which is suff cient to visualize the intermolecular interaction at near atomic level. There are two main factors that cause the advances in cryo-EM; the development of image processing techniques, such as single particle analysis, and the improved electron detection devices. Although the atomic structures of small and asymmetric proteins are not yet to be determined by cryo-EM, this striking improvement implies the bright prospect of the application in biomedical studies. This study reviews the recently published studies reported high resolution structures using improved imaging analysis techniques and electron detectors. Furthermore, we will discuss about the future aspects of cryo-EM application.
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참고문헌 (38)
참고문헌 신청
Allegretti M / 2014 / Atomic model of the F420-reducing [NiFe] hydrogenase by electron cryo-microscopy using a direct electron detector / Elife 3:e01963
Amunts A / 2014 / Structure of the yeast mitochondrial large ribosomal subunit / Science 343:1485~1489
Bai X C / 2015 / How cryo-EM is revolutionizing structural biology / Trends Biochem. Sci 40:49~57
Bartesaghi A / 2014 / Structure of β-galactosidase at 3. 2-Å resolution obtained by cryoelectron microscopy / Proc. Natl. Acad. Sci. USA 111:11709~11714
Bartesaghi A / 2015 / Electron microscopy. 2. 2 Å resolution cryo-EM structure of β-galactosidase in complex with a cell-permeant inhibitor / Science 348:1147~1151
Amunts A / 2014 / Structure of the yeast mitochondrial large ribosomal subunit / Science 343:1485~1489
Bai X C / 2015 / How cryo-EM is revolutionizing structural biology / Trends Biochem. Sci 40:49~57
Bartesaghi A / 2014 / Structure of β-galactosidase at 3. 2-Å resolution obtained by cryoelectron microscopy / Proc. Natl. Acad. Sci. USA 111:11709~11714
Bartesaghi A / 2015 / Electron microscopy. 2. 2 Å resolution cryo-EM structure of β-galactosidase in complex with a cell-permeant inhibitor / Science 348:1147~1151
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