View source for 5amz


==Crystal Structure of Thaumatin processed with the CrystalDirect automated mounting and cryo-cooling technology==
<StructureSection load='5amz' size='340' side='right'caption='[[5amz]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5amz]] 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=5AMZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AMZ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4&#8491;</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=5amz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5amz OCA], [https://pdbe.org/5amz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5amz RCSB], [https://www.ebi.ac.uk/pdbsum/5amz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5amz ProSAT]</span></td></tr>
</table>
== Function ==
[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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== Publication Abstract from PubMed ==
Currently, macromolecular crystallography projects often require the use of highly automated facilities for crystallization and X-ray data collection. However, crystal harvesting and processing largely depend on manual operations. Here, a series of new methods are presented based on the use of a low X-ray-background film as a crystallization support and a photoablation laser that enable the automation of major operations required for the preparation of crystals for X-ray diffraction experiments. In this approach, the controlled removal of the mother liquor before crystal mounting simplifies the cryocooling process, in many cases eliminating the use of cryoprotectant agents, while crystal-soaking experiments are performed through diffusion, precluding the need for repeated sample-recovery and transfer operations. Moreover, the high-precision laser enables new mounting strategies that are not accessible through other methods. This approach bridges an important gap in automation and can contribute to expanding the capabilities of modern macromolecular crystallography facilities.

Automated harvesting and processing of protein crystals through laser photoablation.,Zander U, Hoffmann G, Cornaciu I, Marquette JP, Papp G, Landret C, Seroul G, Sinoir J, Rower M, Felisaz F, Rodriguez-Puente S, Mariaule V, Murphy P, Mathieu M, Cipriani F, Marquez JA Acta Crystallogr D Struct Biol. 2016 Apr 1;72(Pt 4):454-66. doi:, 10.1107/S2059798316000954. Epub 2016 Mar 24. PMID:27050125<ref>PMID:27050125</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 5amz" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thaumatococcus daniellii]]
[[Category: Cipriani F]]
[[Category: Cornaciu I]]
[[Category: Hoffmann G]]
[[Category: Marquez JA]]
[[Category: Zander U]]