4wob: Difference between revisions
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''' | ==Proteinase-K Pre-Surface Acoustic Wave== | ||
<StructureSection load='4wob' size='340' side='right' caption='[[4wob]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4wob]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WOB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WOB FirstGlance]. <br> | |||
</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> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4wo6|4wo6]], [[4wo9|4wo9]], [[4woa|4woa]], [[4woc|4woc]]</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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4wob FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wob OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4wob RCSB], [http://www.ebi.ac.uk/pdbsum/4wob PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/PRTK_ENGAL PRTK_ENGAL]] Hydrolyzes keratin at aromatic and hydrophobic residues. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Advances in modern X-ray sources and detector technology have made it possible for crystallographers to collect usable data on crystals of only a few micrometers or less in size. Despite these developments, sample handling techniques have significantly lagged behind and often prevent the full realization of current beamline capabilities. In order to address this shortcoming, a surface acoustic wave-based method for manipulating and patterning crystals is developed. This method, which does not damage the fragile protein crystals, can precisely manipulate and pattern micrometer and submicrometer-sized crystals for data collection and screening. The technique is robust, inexpensive, and easy to implement. This method not only promises to significantly increase efficiency and throughput of both conventional and serial crystallography experiments, but will also make it possible to collect data on samples that were previously intractable. | |||
Precise Manipulation and Patterning of Protein Crystals for Macromolecular Crystallography Using Surface Acoustic Waves.,Guo F, Zhou W, Li P, Mao Z, Yennawar NH, French JB, Huang TJ Small. 2015 Feb 1. doi: 10.1002/smll.201403262. PMID:25641793<ref>PMID:25641793</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
[[Category: | <references/> | ||
[[Category: French, J | __TOC__ | ||
</StructureSection> | |||
[[Category: Peptidase K]] | |||
[[Category: French, J B]] | |||
[[Category: Acoustic tweezer]] | |||
[[Category: Crystal manipulation]] | |||
[[Category: Nanocrystal]] | |||
[[Category: Serial crystallography]] | |||
[[Category: Surface acoustic wave]] | |||
Revision as of 15:54, 18 February 2015
Proteinase-K Pre-Surface Acoustic WaveProteinase-K Pre-Surface Acoustic Wave
Structural highlights
Function[PRTK_ENGAL] Hydrolyzes keratin at aromatic and hydrophobic residues. Publication Abstract from PubMedAdvances in modern X-ray sources and detector technology have made it possible for crystallographers to collect usable data on crystals of only a few micrometers or less in size. Despite these developments, sample handling techniques have significantly lagged behind and often prevent the full realization of current beamline capabilities. In order to address this shortcoming, a surface acoustic wave-based method for manipulating and patterning crystals is developed. This method, which does not damage the fragile protein crystals, can precisely manipulate and pattern micrometer and submicrometer-sized crystals for data collection and screening. The technique is robust, inexpensive, and easy to implement. This method not only promises to significantly increase efficiency and throughput of both conventional and serial crystallography experiments, but will also make it possible to collect data on samples that were previously intractable. Precise Manipulation and Patterning of Protein Crystals for Macromolecular Crystallography Using Surface Acoustic Waves.,Guo F, Zhou W, Li P, Mao Z, Yennawar NH, French JB, Huang TJ Small. 2015 Feb 1. doi: 10.1002/smll.201403262. PMID:25641793[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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