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Cryomicroscopy development

A completely new method of determining siufaces arises from the enormous developments in electron microscopy. In contrast to the above-mentioned methods where the surfaces were calculated, molecular surfaces can be determined experimentally through new technologies such as electron cryomicroscopy [188]. Here, the molecular surface is limited by the resolution of the experimental instruments. Current methods can reach resolutions down to about 10 A, which allows the visualization of protein structures and secondary structure elements [189]. The advantage of this method is that it can be apphed to derive molecular structures of maaomolecules in the native state. [Pg.129]

Grimes et al., 1998 Reinisch et al, 2000 Wikoff et at, 2000). Likewise, advances in electron cryomicroscopy and image reconstruction techniques allow time-resolved investigations of structural transitions associated with capsid assembly and maturation (Conway et al., 2001 Lawton et al, 1997). These developments have been paralleled by refinements in the molecular approaches used for sample preparation, with the result that synthesis of assembly intermediates and end products has become routine for many viruses. [Pg.2]

Baker, M. L. (2002). Development and Applications of Intermediate Resolution Structural Analysis Tools Integrating Bioinformatics and Electron Cryomicroscopy. Ph.D. thesis. Baylor College of Medicine, Houston, TX. [Pg.404]

The advances in imaging technology have also been applied to cryomicroscopy, in which a simultaneous DSC and optical video instrument has been developed for the characterization of ice crystallization (91). [Pg.261]


See other pages where Cryomicroscopy development is mentioned: [Pg.363]    [Pg.312]    [Pg.251]    [Pg.94]    [Pg.121]    [Pg.1161]    [Pg.11]    [Pg.486]    [Pg.9363]    [Pg.640]    [Pg.2472]   
See also in sourсe #XX -- [ Pg.11 , Pg.12 , Pg.30 ]




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Cryomicroscopy

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