Mancini, Erika J, de Haas, Felix and Fuller, Stephen D (1997) High-resolution icosahedral reconstruction: fulfilling the promise of cryo-electron microscopy. Structure, 5 (6). pp. 741-750. ISSN 0969-2126

Full text not available from this repository.

Abstract

Two recent papers have defined the secondary structure of the hepatitis B virus capsid using a combination of cryoelectron microscopy and icosahedral image reconstruction. These two papers do more than reveal a new fold for a virus protein; they herald a new era in which image reconstruction of single particles will provide reliable high-resolution structural information. In revealing the promise of these techniques to the structural biology community, their two papers should play a seminal role for single particle work, similar to that of the work of Unwin and Henderson [I] on bacteriorhodopsin in revealing the potential of electron microscopy of membrane protein crystals. Indeed, the success of these single particle methods owes much to the development of high-resolution techniques for two-dimensional crystals. This review will summarize some of the history of icosahedral reconstruction from cryo-electron micrographs, compare the two different approaches used to obtain the recent results and outline some of the challenges and promises for the future.

Item Type:	Article
Schools and Departments:	School of Life Sciences > Biochemistry
Subjects:	Q Science
Depositing User:	Tom Gittoes
Date Deposited:	29 Jan 2015 10:32
Last Modified:	29 Jan 2015 10:32
URI:	http://srodev.sussex.ac.uk/id/eprint/52570

📧 Request an update