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2a7e
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==On the Routine Use of Soft X-Rays in Macromolecular Crystallography, Part III- The Optimal Data Collection Wavelength== | ==On the Routine Use of Soft X-Rays in Macromolecular Crystallography, Part III- The Optimal Data Collection Wavelength== | ||
| - | <StructureSection load='2a7e' size='340' side='right' caption='[[2a7e]], [[Resolution|resolution]] 1.66Å' scene=''> | + | <StructureSection load='2a7e' size='340' side='right'caption='[[2a7e]], [[Resolution|resolution]] 1.66Å' scene=''> |
== 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 [ | + | <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'>[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.66Å</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. | ||
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| - | 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> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Mueller-Dieckmann | + | [[Category: Large Structures]] |
| - | [[Category: Panjikar | + | [[Category: Mueller-Dieckmann C]] |
| - | [[Category: Tucker | + | [[Category: Panjikar S]] |
| - | [[Category: Weiss | + | [[Category: Tucker PA]] |
| - | + | [[Category: Weiss MS]] | |
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Current revision
On the Routine Use of Soft X-Rays in Macromolecular Crystallography, Part III- The Optimal Data Collection Wavelength
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