Preservation of high resolution protein structure by cryo-electron microscopy of vitreous sections

Sader, Kasim; Studer, Daniel; Zuber, Benoît; Gnaegi, Helmut; Trinick, John (2009). Preservation of high resolution protein structure by cryo-electron microscopy of vitreous sections. Ultramicroscopy, 110(1), pp. 43-7. New York, N.Y.: Elsevier 10.1016/j.ultramic.2009.09.004

Full text not available from this repository.

We have quantitated the degree of structural preservation in cryo-sections of a vitrified biological specimen. Previous studies have used sections of periodic specimens to assess the resolution present, but preservation before sectioning was not assessed and so the damage due particularly to cutting was not clear. In this study large single crystals of lysozyme were vitrified and from these X-ray diffraction patterns extending to better than 2.1A were obtained. The crystals were high pressure frozen in 30% dextran, and cryo-sectioned using a diamond knife. In the best case, preservation to a resolution of 7.9A was shown by electron diffraction, the first observation of sub-nanometre structural preservation in a vitreous section.

Item Type:	Journal Article (Original Article)
Division/Institute:	04 Faculty of Medicine > Pre-clinic Human Medicine > Institute of Anatomy
UniBE Contributor:	Studer, Daniel Franz, Zuber, Benoît
Subjects:	600 Technology > 610 Medicine & health
ISSN:	0304-3991
Publisher:	Elsevier
Language:	English
Submitter:	Benoît Zuber
Date Deposited:	04 Oct 2013 15:11
Last Modified:	05 Dec 2022 14:21
Publisher DOI:	10.1016/j.ultramic.2009.09.004
PubMed ID:	19819624
Web of Science ID:	000272733400007
URI:	https://boris.unibe.ch/id/eprint/31081 (FactScience: 195484)