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	<id>https://3demmethods.i2pc.es/index.php?action=history&amp;feed=atom&amp;title=2005Steven_Review</id>
	<title>2005Steven Review - Revision history</title>
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	<updated>2026-05-24T20:36:36Z</updated>
	<subtitle>Revision history for this page on the wiki</subtitle>
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	<entry>
		<id>https://3demmethods.i2pc.es/index.php?title=2005Steven_Review&amp;diff=2737&amp;oldid=prev</id>
		<title>CoSS: Created page with &quot;== Citation ==  Steven, A. &amp; Belnap, D. Electron microscopy and image processing: an essential tool for structural analysis of macromolecules. Curr Protoc Protein Sci, 2005, C...&quot;</title>
		<link rel="alternate" type="text/html" href="https://3demmethods.i2pc.es/index.php?title=2005Steven_Review&amp;diff=2737&amp;oldid=prev"/>
		<updated>2015-11-05T10:08:54Z</updated>

		<summary type="html">&lt;p&gt;Created page with &amp;quot;== Citation ==  Steven, A. &amp;amp; Belnap, D. Electron microscopy and image processing: an essential tool for structural analysis of macromolecules. Curr Protoc Protein Sci, 2005, C...&amp;quot;&lt;/p&gt;
&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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Steven, A. &amp;amp; Belnap, D. Electron microscopy and image processing: an essential tool for structural analysis of macromolecules. Curr Protoc Protein Sci, 2005, Chapter 17, Unit 17.2&lt;br /&gt;
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== Abstract ==&lt;br /&gt;
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Macromolecular electron microscopy (EM) deals with macromolecular complexes and their placement within the cell-linking the molecular and cellular worlds as a bridge between atomic-resolution X-ray crystallographic or NMR studies and lower resolution light microscopy. The amount of specimen required is typically 10(2) to 10(3) times less than for X-ray crystallography or NMR. Electron micrographs of frozen-hydrated specimens portray native structures. Computer averaging yields enhanced images with reduced noise. Three-dimensional reconstructions may be computed from multiple views. Under favorable circumstances, resolutions of 7 to 10 A are achieved. Fitting atomic-resolution coordinates of components into three-dimensional density maps gives pseudo-atomic models of a complex&amp;#039;s structure and interactions. Time-resolved experiments describe conformational changes. Electron tomography allows reconstruction of pleiomorphic complexes and sub-cellular structures. Electron crystallography has produced near-atomic resolution models of two-dimensional arrays, notably of membrane proteins.&lt;br /&gt;
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== Keywords ==&lt;br /&gt;
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== Links ==&lt;br /&gt;
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http://onlinelibrary.wiley.com/doi/10.1002/0471140864.ps1702s42/abstract;jsessionid=E562C32176D0AAB1E7BD651671088FC6.f04t03&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>CoSS</name></author>
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