2a7e: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2a7e]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A7E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2A7E FirstGlance]. <br>
<table><tr><td colspan='2'>[[2a7e]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A7E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2A7E FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2a7e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a7e OCA], [https://pdbe.org/2a7e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a7e RCSB], [https://www.ebi.ac.uk/pdbsum/2a7e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a7e ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.66&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2a7e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a7e OCA], [https://pdbe.org/2a7e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a7e RCSB], [https://www.ebi.ac.uk/pdbsum/2a7e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a7e ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Complete and highly redundant data sets were collected at different wavelengths between 0.80 and 2.65 A for a total of ten different protein and DNA model systems. The magnitude of the anomalous signal-to-noise ratio as assessed by the quotient R(anom)/R(r.i.m.) was found to be influenced by the data-collection wavelength and the nature of the anomalously scattering substructure. By utilizing simple empirical correlations, for instance between the estimated deltaF/F and the expected R(anom) or the data-collection wavelength and the expected R(r.i.m.), the wavelength at which the highest anomalous signal-to-noise ratio can be expected could be estimated even before the experiment. Almost independent of the nature of the anomalously scattering substructure and provided that no elemental X-ray absorption edge is nearby, this optimal wavelength is 2.1 A.
On the routine use of soft X-rays in macromolecular crystallography. Part III. The optimal data-collection wavelength.,Mueller-Dieckmann C, Panjikar S, Tucker PA, Weiss MS Acta Crystallogr D Biol Crystallogr. 2005 Sep;61(Pt 9):1263-72. Epub 2005, Aug 16. PMID:16131760<ref>PMID:16131760</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2a7e" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Mueller-Dieckmann, C]]
[[Category: Mueller-Dieckmann C]]
[[Category: Panjikar, S]]
[[Category: Panjikar S]]
[[Category: Tucker, P A]]
[[Category: Tucker PA]]
[[Category: Weiss, M S]]
[[Category: Weiss MS]]
[[Category: A-dna]]
[[Category: Dna]]
[[Category: Double helix]]
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