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		<title>WikiSysop at 06:38, 22 December 2010</title>
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		<summary type="html">&lt;p&gt;&lt;/p&gt;
&lt;p&gt;&lt;b&gt;New page&lt;/b&gt;&lt;/p&gt;&lt;div&gt;== Citation ==&lt;br /&gt;
&lt;br /&gt;
Studer, D.; Humbel, B. M. &amp;amp; Chiquet, M. Electron microscropy of high pressure frozen samples: bridging the gap between cellular ultrastructure and atomic resolution. Histochem. Cell Biology, 2008, 130, 877-889&lt;br /&gt;
&lt;br /&gt;
[http://scholar.google.es/scholar?cites=17961457282287549388 Cited by]&lt;br /&gt;
&lt;br /&gt;
== Abstract ==&lt;br /&gt;
&lt;br /&gt;
Transmission electron microscopy has provided&lt;br /&gt;
most of what is known about the ultrastructural organization&lt;br /&gt;
of tissues, cells, and organelles. Due to tremendous&lt;br /&gt;
advances in crystallography and magnetic resonance imaging,&lt;br /&gt;
almost any protein can now be modeled at atomic resolution.&lt;br /&gt;
To fully understand the workings of biological&lt;br /&gt;
“nanomachines” it is necessary to obtain images of intact&lt;br /&gt;
macromolecular assemblies in situ. Although the resolution&lt;br /&gt;
power of electron microscopes is on the atomic scale, in&lt;br /&gt;
biological samples artifacts introduced by aldehyde Wxation,&lt;br /&gt;
dehydration and staining, but also section thickness&lt;br /&gt;
reduces it to some nanometers. CryoWxation by high pressure&lt;br /&gt;
freezing circumvents many of the artifacts since it&lt;br /&gt;
allows vitrifying biological samples of about 200 �m in&lt;br /&gt;
thickness and immobilizes complex macromolecular&lt;br /&gt;
assemblies in their native state in situ. To exploit the perfect&lt;br /&gt;
structural preservation of frozen hydrated sections,&lt;br /&gt;
sophisticated instruments are needed, e.g., high voltage&lt;br /&gt;
electron microscopes equipped with precise goniometers&lt;br /&gt;
that work at low temperature and digital cameras of high&lt;br /&gt;
sensitivity and pixel number. With them, it is possible to&lt;br /&gt;
generate high resolution tomograms, i.e., 3D views of subcellular&lt;br /&gt;
structures. This review describes theory and applications&lt;br /&gt;
of the high pressure cryoWxation methodology and&lt;br /&gt;
compares its results with those of conventional procedures.&lt;br /&gt;
Moreover, recent Wndings will be discussed showing that&lt;br /&gt;
molecular models of proteins can be Wtted into depicted&lt;br /&gt;
organellar ultrastructure of images of frozen hydrated sections.&lt;br /&gt;
High pressure freezing of tissue is the base which&lt;br /&gt;
may lead to precise models of macromolecular assemblies&lt;br /&gt;
in situ, and thus to a better understanding of the function of&lt;br /&gt;
complex cellular structures.&lt;br /&gt;
&lt;br /&gt;
== Keywords ==&lt;br /&gt;
&lt;br /&gt;
High pressure freezing, sample preparation&lt;br /&gt;
&lt;br /&gt;
== Links ==&lt;br /&gt;
&lt;br /&gt;
Article http://www.springerlink.com/content/37462742334747v6/&lt;br /&gt;
&lt;br /&gt;
== Related software ==&lt;br /&gt;
&lt;br /&gt;
== Related methods ==&lt;br /&gt;
&lt;br /&gt;
== Comments ==&lt;/div&gt;</summary>
		<author><name>WikiSysop</name></author>
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