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Affinity cryo-electron microscopy: M...

Yu, Guimei.

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Affinity cryo-electron microscopy: Methods development and applications.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Affinity cryo-electron microscopy: Methods development and applications./
Author:	Yu, Guimei.
Published:	Ann Arbor : ProQuest Dissertations & Theses, : 2016,
Description:	148 p.
Notes:	Source: Dissertation Abstracts International, Volume: 77-12(E), Section: B.
Contained By:	Dissertation Abstracts International77-12B(E).
Subject:	Molecular biology. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=10149196
ISBN:	9781369043143

Affinity cryo-electron microscopy: Methods development and applications.
Yu, Guimei.

Affinity cryo-electron microscopy: Methods development and applications. - Ann Arbor : ProQuest Dissertations & Theses, 2016 - 148 p.

Source: Dissertation Abstracts International, Volume: 77-12(E), Section: B.

Thesis (Ph.D.)--Purdue University, 2016.

This item is not available from ProQuest Dissertations & Theses.

Single particle cryo-electron microscopy (cryo-EM) is an emerging powerful tool for structural studies of macromolecular assemblies. Although less concentrated and smaller amounts of samples are required for single particle cryo-EM compared to X-ray crystallography, it remains challenging to study specimens that are low-abundance, low-yield, or short-lived. The recent development of affinity grid techniques holds great promise to tackle these challenging samples by combining the sample purification and freezing on TEM grids steps in cryo-EM grid preparation into a single step, revolutionize the grid preparation of cryo-EM, and extend single particle cryo-EM to a routine structural biology tool to characterize structures of a broad spectrum of macromolecules.

ISBN: 9781369043143Subjects--Topical Terms:

517296
Molecular biology.

Affinity cryo-electron microscopy: Methods development and applications.
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100 1 $a Yu, Guimei. $3 3285924
245 1 0 $a Affinity cryo-electron microscopy: Methods development and applications.
260 1 $a Ann Arbor : $b ProQuest Dissertations & Theses, $c 2016
300 $a 148 p.
500 $a Source: Dissertation Abstracts International, Volume: 77-12(E), Section: B.
500 $a Adviser: Wen Jiang.
502 $a Thesis (Ph.D.)--Purdue University, 2016.
506 $a This item is not available from ProQuest Dissertations & Theses.
520 $a Single particle cryo-electron microscopy (cryo-EM) is an emerging powerful tool for structural studies of macromolecular assemblies. Although less concentrated and smaller amounts of samples are required for single particle cryo-EM compared to X-ray crystallography, it remains challenging to study specimens that are low-abundance, low-yield, or short-lived. The recent development of affinity grid techniques holds great promise to tackle these challenging samples by combining the sample purification and freezing on TEM grids steps in cryo-EM grid preparation into a single step, revolutionize the grid preparation of cryo-EM, and extend single particle cryo-EM to a routine structural biology tool to characterize structures of a broad spectrum of macromolecules.
520 $a In my PhD study, I have established a new design of the affinity cryo-EM approach, cryo-SPIEM that applies a traditional pathogen diagnosis tool Solid Phase Immune Electron Microscopy (SPIEM) to the single particle cryo-EM method, and also systematically explored the applications of affinity EM approaches and the potentials of affinity cryo-EM approaches for near-atomic single particle 3-D reconstruction. The cryo-SPIEM approach provides an alternative, largely simplified and easier to use affinity grid that directly works with most native macromolecular complexes with established antibodies, and enables cryo-EM studies of native samples directly from cell cultures. The application of the affinity cryo-EM approach for high-resolution cryo-EM has been demonstrated successfully by solving a 6.3 A structure of Tulane virus using the polylysine-based affinity grid, and a 2.6 A structure of Tulane virus using the antibody-based affinity grid with a sample of low concentrations that defies standard cryo-EM study. Moreover, we have applied the affinity grid technique to investigate the interaction between Tulane virus and its cellular receptor Histo-blood group antigens, which revealed the potential roles of HBGA receptors in mediating genome release.
590 $a School code: 0183.
650 4 $a Molecular biology. $3 517296
650 4 $a Biophysics. $3 518360
650 4 $a Microbiology. $3 536250
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710 2 $a Purdue University. $b Biological Sciences. $3 1285872
773 0 $t Dissertation Abstracts International $g 77-12B(E).
790 $a 0183
791 $a Ph.D.
792 $a 2016
793 $a English
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=10149196