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| | ==Thaumatin structure determined at room temperature by in-situ diffraction in ChipX== | | ==Thaumatin structure determined at room temperature by in-situ diffraction in ChipX== |
| - | <StructureSection load='3zej' size='340' side='right' caption='[[3zej]], [[Resolution|resolution]] 1.55Å' scene=''> | + | <StructureSection load='3zej' size='340' side='right'caption='[[3zej]], [[Resolution|resolution]] 1.55Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3zej]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/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> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.55Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3zek|3zek]]</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> |
| - | <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=3zej FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zej OCA], [http://pdbe.org/3zej PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3zej RCSB], [http://www.ebi.ac.uk/pdbsum/3zej PDBsum], [http://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 == |
| - | [[http://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. | + | [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. |
| - | <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®/PubMed®, 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: Thaumatococcus daniellii]] | | [[Category: Thaumatococcus daniellii]] |
| - | [[Category: Lorber, B]] | + | [[Category: Lorber B]] |
| - | [[Category: Pinker, F]] | + | [[Category: Pinker F]] |
| - | [[Category: Sauter, C]] | + | [[Category: Sauter C]] |
| - | [[Category: Microfluidic chip]]
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| - | [[Category: Plant protein]]
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