6m9b

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Current revision (14:41, 13 March 2024) (edit) (undo)
 
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<StructureSection load='6m9b' size='340' side='right'caption='[[6m9b]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
<StructureSection load='6m9b' size='340' side='right'caption='[[6m9b]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6m9b]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/As_4.1583 As 4.1583]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6M9B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6M9B FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6m9b]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_avidinii Streptomyces avidinii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6M9B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6M9B FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BTN:BIOTIN'>BTN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.548&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6m9b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6m9b OCA], [http://pdbe.org/6m9b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6m9b RCSB], [http://www.ebi.ac.uk/pdbsum/6m9b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6m9b ProSAT]</span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BTN:BIOTIN'>BTN</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6m9b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6m9b OCA], [https://pdbe.org/6m9b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6m9b RCSB], [https://www.ebi.ac.uk/pdbsum/6m9b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6m9b ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/SAV_STRAV SAV_STRAV]] The biological function of streptavidin is not known. Forms a strong non-covalent specific complex with biotin (one molecule of biotin per subunit of streptavidin).
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[https://www.uniprot.org/uniprot/SAV_STRAV SAV_STRAV] The biological function of streptavidin is not known. Forms a strong non-covalent specific complex with biotin (one molecule of biotin per subunit of streptavidin).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Native single-wavelength anomalous dispersion (SAD) is the most attractive de novo phasing method in macromolecular crystallography, as it directly utilizes intrinsic anomalous scattering from native crystals. However, the success of such an experiment depends on accurate measurements of the reflection intensities and therefore on careful data-collection protocols. Here, the low-dose, multiple-orientation data-collection protocol for native SAD phasing developed at beamline X06DA (PXIII) at the Swiss Light Source is reviewed, and its usage over the last four years on conventional crystals (&gt;50 microm) is reported. Being experimentally very simple and fast, this method has gained popularity and has delivered 45 de novo structures to date (13 of which have been published). Native SAD is currently the primary choice for experimental phasing among X06DA users. The method can address challenging cases: here, native SAD phasing performed on a streptavidin-biotin crystal with P21 symmetry and a low Bijvoet ratio of 0.6% is highlighted. The use of intrinsic anomalous signals as sequence markers for model building and the assignment of ions is also briefly described.
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Making routine native SAD a reality: lessons from beamline X06DA at the Swiss Light Source.,Basu S, Finke A, Vera L, Wang M, Olieric V Acta Crystallogr D Struct Biol. 2019 Mar 1;75(Pt 3):262-271. doi:, 10.1107/S2059798319003103. Epub 2019 Mar 12. PMID:30950397<ref>PMID:30950397</ref>
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==See Also==
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*[[Avidin 3D structures|Avidin 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6m9b" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: As 4 1583]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Finke, A D]]
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[[Category: Streptomyces avidinii]]
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[[Category: Biotin binder]]
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[[Category: Finke AD]]
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[[Category: Ligand]]
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[[Category: Structural protein]]
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[[Category: Tetramer]]
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[[Category: Wild type]]
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Current revision

Wild-type streptavidin in complex with biotin solved by native SAD with data collected at 6 keV

PDB ID 6m9b

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