5amx: Difference between revisions
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==Crystal Structure of Proteinase K processed with the CrystalDirect automated mounting and cryo-cooling technology== | ==Crystal Structure of Proteinase K processed with the CrystalDirect automated mounting and cryo-cooling technology== | ||
<StructureSection load='5amx' size='340' side='right' caption='[[5amx]], [[Resolution|resolution]] 1.01Å' scene=''> | <StructureSection load='5amx' size='340' side='right'caption='[[5amx]], [[Resolution|resolution]] 1.01Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5amx]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5amx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Parengyodontium_album Parengyodontium album]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AMX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AMX FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.01Å</td></tr> | ||
<tr id=' | <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'>[https://proteopedia.org/fgij/fg.htm?mol=5amx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5amx OCA], [https://pdbe.org/5amx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5amx RCSB], [https://www.ebi.ac.uk/pdbsum/5amx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5amx ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/PRTK_PARAQ PRTK_PARAQ] Hydrolyzes keratin at aromatic and hydrophobic residues. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 24: | Line 23: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Parengyodontium album]] | ||
[[Category: Cipriani | [[Category: Cipriani F]] | ||
[[Category: Cornaciu | [[Category: Cornaciu I]] | ||
[[Category: Hoffmann | [[Category: Hoffmann G]] | ||
[[Category: Marquez | [[Category: Marquez JA]] | ||
[[Category: Zander | [[Category: Zander U]] | ||
Latest revision as of 11:42, 23 October 2024
Crystal Structure of Proteinase K processed with the CrystalDirect automated mounting and cryo-cooling technologyCrystal Structure of Proteinase K processed with the CrystalDirect automated mounting and cryo-cooling technology
Structural highlights
FunctionPRTK_PARAQ Hydrolyzes keratin at aromatic and hydrophobic residues. Publication Abstract from PubMedCurrently, 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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