6zev: Difference between revisions
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==Crystal structure of proteinase K lamellae by electron diffraction with a 20 micrometre C2 condenser aperture== | ==Crystal structure of proteinase K lamellae by electron diffraction with a 20 micrometre C2 condenser aperture== | ||
<StructureSection load='6zev' size='340' side='right'caption='[[6zev]]' scene=''> | <StructureSection load='6zev' size='340' side='right'caption='[[6zev]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZEV OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6ZEV FirstGlance]. <br> | <table><tr><td colspan='2'>[[6zev]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZEV OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6ZEV FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6zev FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zev OCA], [http://pdbe.org/6zev PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6zev RCSB], [http://www.ebi.ac.uk/pdbsum/6zev PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6zev ProSAT]</span></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | ||
<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> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6zev FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zev OCA], [http://pdbe.org/6zev PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6zev RCSB], [http://www.ebi.ac.uk/pdbsum/6zev PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6zev ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/PRTK_PARAQ PRTK_PARAQ]] Hydrolyzes keratin at aromatic and hydrophobic residues. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
MicroED has recently emerged as a powerful method for the analysis of biological structures at atomic resolution. This technique has been largely limited to protein nanocrystals which grow either as needles or plates measuring only a few hundred nanometers in thickness. Furthermore, traditional microED data processing uses established X-ray crystallography software that is not optimized for handling compound effects that are unique to electron diffraction data. Here, we present an integrated workflow for microED, from sample preparation by cryo-focused ion beam milling, through data collection with a standard Ceta-D detector, to data processing using the DIALS software suite, thus enabling routine atomic structure determination of protein crystals of any size and shape using microED. We demonstrate the effectiveness of the workflow by determining the structure of proteinase K to 2.0 A resolution and show the advantage of using protein crystal lamellae over nanocrystals. | |||
A Workflow for Protein Structure Determination From Thin Crystal Lamella by Micro-Electron Diffraction.,Beale EV, Waterman DG, Hecksel C, van Rooyen J, Gilchrist JB, Parkhurst JM, de Haas F, Buijsse B, Evans G, Zhang P Front Mol Biosci. 2020 Aug 4;7:179. doi: 10.3389/fmolb.2020.00179. eCollection, 2020. PMID:32850967<ref>PMID:32850967</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6zev" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Beale | [[Category: Peptidase K]] | ||
[[Category: Evans G]] | [[Category: Beale, E V]] | ||
[[Category: Waterman | [[Category: Evans, G]] | ||
[[Category: Zhang P]] | [[Category: Waterman, D G]] | ||
[[Category: Zhang, P]] | |||
[[Category: Hydrolase]] | |||
[[Category: Protease]] | |||
[[Category: Serine protease]] | |||
Revision as of 10:14, 25 November 2020
Crystal structure of proteinase K lamellae by electron diffraction with a 20 micrometre C2 condenser apertureCrystal structure of proteinase K lamellae by electron diffraction with a 20 micrometre C2 condenser aperture
Structural highlights
Function[PRTK_PARAQ] Hydrolyzes keratin at aromatic and hydrophobic residues. Publication Abstract from PubMedMicroED has recently emerged as a powerful method for the analysis of biological structures at atomic resolution. This technique has been largely limited to protein nanocrystals which grow either as needles or plates measuring only a few hundred nanometers in thickness. Furthermore, traditional microED data processing uses established X-ray crystallography software that is not optimized for handling compound effects that are unique to electron diffraction data. Here, we present an integrated workflow for microED, from sample preparation by cryo-focused ion beam milling, through data collection with a standard Ceta-D detector, to data processing using the DIALS software suite, thus enabling routine atomic structure determination of protein crystals of any size and shape using microED. We demonstrate the effectiveness of the workflow by determining the structure of proteinase K to 2.0 A resolution and show the advantage of using protein crystal lamellae over nanocrystals. A Workflow for Protein Structure Determination From Thin Crystal Lamella by Micro-Electron Diffraction.,Beale EV, Waterman DG, Hecksel C, van Rooyen J, Gilchrist JB, Parkhurst JM, de Haas F, Buijsse B, Evans G, Zhang P Front Mol Biosci. 2020 Aug 4;7:179. doi: 10.3389/fmolb.2020.00179. eCollection, 2020. PMID:32850967[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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