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==Native-SAD phasing for ThiT from Listeria monocytogenes serovar.== | ==Native-SAD phasing for ThiT from Listeria monocytogenes serovar.== | ||
<StructureSection load='4tkr' size='340' side='right' caption='[[4tkr]], [[Resolution|resolution]] 3.00Å' scene=''> | <StructureSection load='4tkr' size='340' side='right'caption='[[4tkr]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4tkr]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TKR OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[4tkr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TKR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TKR FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGL:B-2-OCTYLGLUCOSIDE'>BGL</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene>< | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.0023Å</td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGL:B-2-OCTYLGLUCOSIDE'>BGL</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene></td></tr> | ||
<table> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4tkr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tkr OCA], [https://pdbe.org/4tkr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tkr RCSB], [https://www.ebi.ac.uk/pdbsum/4tkr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tkr ProSAT]</span></td></tr> | ||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A0B8R2U7_LISMN A0A0B8R2U7_LISMN] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Anomalous diffraction signals from typical native macromolecules are very weak, frustrating their use in de novo structure determination. Here, native SAD procedures are described to enhance signal to noise in anomalous diffraction by using multiple crystals in combination with synchrotron X-rays at 6 keV. Increased anomalous signals were obtained at 6 keV compared with 7 keV X-ray energy, which was used for previous native SAD analyses. A feasibility test of multi-crystal-based native SAD phasing was performed at 3.2 A resolution for a known tyrosine protein kinase domain, and real-life applications were made to two novel membrane proteins at about 3.0 A resolution. The three applications collectively serve to validate the robust feasibility of native SAD phasing at lower energy. | |||
Multi-crystal native SAD analysis at 6 keV.,Liu Q, Guo Y, Chang Y, Cai Z, Assur Z, Mancia F, Greene MI, Hendrickson WA Acta Crystallogr D Biol Crystallogr. 2014 Oct 1;70(Pt 10):2544-57. doi:, 10.1107/S1399004714013376. Epub 2014 Sep 30. PMID:25286840<ref>PMID:25286840</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4tkr" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Listeria monocytogenes]] | ||
[[Category: | [[Category: Guo Y]] | ||
[[Category: | [[Category: Hendrickson WA]] | ||
[[Category: | [[Category: Liu Q]] | ||
Latest revision as of 03:46, 28 December 2023
Native-SAD phasing for ThiT from Listeria monocytogenes serovar.Native-SAD phasing for ThiT from Listeria monocytogenes serovar.
Structural highlights
FunctionPublication Abstract from PubMedAnomalous diffraction signals from typical native macromolecules are very weak, frustrating their use in de novo structure determination. Here, native SAD procedures are described to enhance signal to noise in anomalous diffraction by using multiple crystals in combination with synchrotron X-rays at 6 keV. Increased anomalous signals were obtained at 6 keV compared with 7 keV X-ray energy, which was used for previous native SAD analyses. A feasibility test of multi-crystal-based native SAD phasing was performed at 3.2 A resolution for a known tyrosine protein kinase domain, and real-life applications were made to two novel membrane proteins at about 3.0 A resolution. The three applications collectively serve to validate the robust feasibility of native SAD phasing at lower energy. Multi-crystal native SAD analysis at 6 keV.,Liu Q, Guo Y, Chang Y, Cai Z, Assur Z, Mancia F, Greene MI, Hendrickson WA Acta Crystallogr D Biol Crystallogr. 2014 Oct 1;70(Pt 10):2544-57. doi:, 10.1107/S1399004714013376. Epub 2014 Sep 30. PMID:25286840[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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