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		<title>WikiSysop at 06:42, 30 April 2009</title>
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&lt;p&gt;&lt;b&gt;New page&lt;/b&gt;&lt;/p&gt;&lt;div&gt;== Citation ==&lt;br /&gt;
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Frangakis AS, Bohm J, Forster F, Nickell S, Nicastro D, Typke D,&lt;br /&gt;
Hegerl R, Baumeister W (2002) Identification of macromolecular&lt;br /&gt;
complexes in cryoelectron tomograms of phantom cells. Proc&lt;br /&gt;
Natl Acad Sci USA 99:14153–14158&lt;br /&gt;
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[http://scholar.google.es/scholar?hl=en&amp;amp;lr=&amp;amp;cites=9982414801760274439 Cited by]&lt;br /&gt;
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== Abstract ==&lt;br /&gt;
&lt;br /&gt;
Electron tomograms of intact frozen-hydrated cells are essentially three-dimensional images of the entire proteome of the cell, and they depict the whole network of macromolecular interactions. However, this information is not easily accessible because of the poor signal-to-noise ratio of the tomograms and the crowded nature of the cytoplasm. Here, we describe a template matching algorithm that is capable of detecting and identifying macromolecules in tomographic volumes in a fully automated manner. The algorithm is based on nonlinear cross correlation and incorporates elements of multivariate statistical analysis. Phantom cells, i.e., lipid vesicles filled with macromolecules, provide a realistic experimental scenario for an assessment of the fidelity of this approach. At the current resolution of approximately 4 nm, macromolecules in the size range of 0.5-1 MDa can be identified with good fidelity.&lt;br /&gt;
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== Keywords ==&lt;br /&gt;
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Electron tomography, single particles, localization&lt;br /&gt;
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== Links ==&lt;br /&gt;
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Article http://www.ncbi.nlm.nih.gov/pubmed/12391313&lt;br /&gt;
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== Related software ==&lt;br /&gt;
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== Related methods ==&lt;br /&gt;
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== Comments ==&lt;/div&gt;</summary>
		<author><name>WikiSysop</name></author>
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