3zej

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3zej]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thaumatococcus_daniellii Thaumatococcus daniellii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZEJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZEJ FirstGlance]. <br>
<table><tr><td colspan='2'>[[3zej]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thaumatococcus_daniellii Thaumatococcus daniellii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZEJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZEJ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</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]] 1.55&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3zek|3zek]]</div></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=TLA:L(+)-TARTARIC+ACID'>TLA</scene></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=3zej FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zej OCA], [https://pdbe.org/3zej PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zej RCSB], [https://www.ebi.ac.uk/pdbsum/3zej PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zej ProSAT]</span></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=3zej FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zej OCA], [https://pdbe.org/3zej PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zej RCSB], [https://www.ebi.ac.uk/pdbsum/3zej PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zej ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/THM1_THADA THM1_THADA]] Taste-modifying protein; intensely sweet-tasting. It is 100000 times sweeter than sucrose on a molar basis.
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[https://www.uniprot.org/uniprot/THM1_THADA THM1_THADA] Taste-modifying protein; intensely sweet-tasting. It is 100000 times sweeter than sucrose on a molar basis.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Microfluidic devices were designed to perform on micromoles of biological macromolecules and viruses the search and the optimization of crystallization conditions by counter-diffusion, as well as the on-chip analysis of crystals by X-ray diffraction. Chips composed of microchannels were fabricated in poly-dimethylsiloxane (PDMS), poly-methyl-methacrylate (PMMA) and cyclo-olefin-copolymer (COC) by three distinct methods, namely replica casting, laser ablation and hot embossing. The geometry of the channels was chosen to ensure that crystallization occurs in a convection-free environment. The transparency of the materials is compatible with crystal growth monitoring by optical microscopy. The quality of the protein 3D structures derived from on-chip crystal analysis by X-ray diffraction using a synchrotron radiation was used to identify the most appropriate polymers. Altogether the results demonstrate that for a novel biomolecule, all steps from the initial search of crystallization conditions to X-ray diffraction data collection for 3D structure determination can be performed in a single chip.
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Microfluidic chips for the crystallization of biomacromolecules by counter-diffusion and on-chip crystal X-ray analysis.,Dhouib K, Khan Malek C, Pfleging W, Gauthier-Manuel B, Duffait R, Thuillier G, Ferrigno R, Jacquamet L, Ohana J, Ferrer JL, Theobald-Dietrich A, Giege R, Lorber B, Sauter C Lab Chip. 2009 May 21;9(10):1412-21. doi: 10.1039/b819362b. Epub 2009 Mar 2. PMID:19417908<ref>PMID:19417908</ref>
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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 3zej" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Thaumatococcus daniellii]]
[[Category: Thaumatococcus daniellii]]
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[[Category: Lorber, B]]
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[[Category: Lorber B]]
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[[Category: Pinker, F]]
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[[Category: Pinker F]]
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[[Category: Sauter, C]]
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[[Category: Sauter C]]
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[[Category: Microfluidic chip]]
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[[Category: Plant protein]]
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Current revision

Thaumatin structure determined at room temperature by in-situ diffraction in ChipX

PDB ID 3zej

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