5nlu: Difference between revisions
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==Structure of Nb36 crystal form 1== | ==Structure of Nb36 crystal form 1== | ||
<StructureSection load='5nlu' size='340' side='right' caption='[[5nlu]], [[Resolution|resolution]] 1.19Å' scene=''> | <StructureSection load='5nlu' size='340' side='right'caption='[[5nlu]], [[Resolution|resolution]] 1.19Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5nlu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Camelus_glama Camelus glama]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NLU OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[5nlu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Camelus_glama Camelus glama]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NLU OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5NLU FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5nlu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nlu OCA], [http://pdbe.org/5nlu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nlu RCSB], [http://www.ebi.ac.uk/pdbsum/5nlu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nlu ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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</div> | </div> | ||
<div class="pdbe-citations 5nlu" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5nlu" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Antibody 3D structures|Antibody 3D structures]] | |||
*[[3D structures of non-human antibody|3D structures of non-human antibody]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Camelus glama]] | [[Category: Camelus glama]] | ||
[[Category: Large Structures]] | |||
[[Category: Andersen, G R]] | [[Category: Andersen, G R]] | ||
[[Category: Andersen, K R]] | [[Category: Andersen, K R]] | ||
Revision as of 15:07, 26 August 2020
Structure of Nb36 crystal form 1Structure of Nb36 crystal form 1
Structural highlights
Publication Abstract from PubMedThe generation of high-quality protein crystals and the loss of phase information during an X-ray crystallography diffraction experiment represent the major bottlenecks in the determination of novel protein structures. A generic method for introducing Hg atoms into any crystal independent of the presence of free cysteines in the target protein could considerably facilitate the process of obtaining unbiased experimental phases. Nanobodies (single-domain antibodies) have recently been shown to promote the crystallization and structure determination of flexible proteins and complexes. To extend the usability of nanobodies for crystallographic work, variants of the Nb36 nanobody with a single free cysteine at one of four framework-residue positions were developed. These cysteines could be labelled with fluorophores or Hg. For one cysteine variant (Nb36-C85) two nanobody structures were experimentally phased using single-wavelength anomalous dispersion (SAD) and single isomorphous replacement with anomalous signal (SIRAS), taking advantage of radiation-induced changes in Cys-Hg bonding. Importantly, Hg labelling influenced neither the interaction of Nb36 with its antigen complement C5 nor its structure. The results suggest that Cys-Hg-labelled nanobodies may become efficient tools for obtaining de novo phase information during the structure determination of nanobody-protein complexes. Introducing site-specific cysteines into nanobodies for mercury labelling allows de novo phasing of their crystal structures.,Hansen SB, Laursen NS, Andersen GR, Andersen KR Acta Crystallogr D Struct Biol. 2017 Oct 1;73(Pt 10):804-813. doi:, 10.1107/S2059798317013171. Epub 2017 Sep 27. PMID:28994409[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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