6law

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'''Unreleased structure'''
 
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The entry 6law is ON HOLD
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==MicroED structure of proteinase K at 1.50A determained using crystal lamellas prepared by focused ion beam milling==
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<StructureSection load='6law' size='340' side='right'caption='[[6law]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6law]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Parengyodontium_album Parengyodontium album]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LAW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6LAW FirstGlance]. <br>
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</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>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidase_K Peptidase K], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.64 3.4.21.64] </span></td></tr>
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<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=6law FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6law OCA], [http://pdbe.org/6law PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6law RCSB], [http://www.ebi.ac.uk/pdbsum/6law PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6law ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/PRTK_PARAQ PRTK_PARAQ]] Hydrolyzes keratin at aromatic and hydrophobic residues.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Electron diffraction provides a powerful tool to solve the structures of small protein crystals. However, strong interactions between the electrons and the materials limit the application of the electron crystallographic method on large protein crystals with micrometer or larger sizes. Here, we used the focused ion beam (FIB) equipped on the scanning electron microscope (SEM) to mill a large crystal to thin lamella. The influences of the milling on the crystal lamella were observed and investigated, including radiation damage on the crystal surface during the FIB imaging, deformation of the thin crystal lamella, and variation in the diffraction intensities under electron radiation. These observations provide important information to optimize the FIB milling, and hence is important to obtain high-quality crystal samples for routine structure determination of protein crystals using the electron cryo-microscope.
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Authors:
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Using focus ion beam to prepare crystal lamella for electron diffraction.,Zhou H, Luo Z, Li X J Struct Biol. 2019 Mar 1;205(3):59-64. doi: 10.1016/j.jsb.2019.02.004. Epub 2019, Feb 20. PMID:30794865<ref>PMID:30794865</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 6law" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Parengyodontium album]]
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[[Category: Peptidase K]]
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[[Category: Li, X]]
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[[Category: Luo, Z]]
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[[Category: Zhou, H]]
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[[Category: Crystal lamella]]
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[[Category: Focused ion beam]]
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[[Category: Hydrolase]]
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[[Category: Microed]]
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[[Category: Proteinase k]]

Revision as of 08:07, 4 December 2019

MicroED structure of proteinase K at 1.50A determained using crystal lamellas prepared by focused ion beam milling

PDB ID 6law

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