2oqu: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2oqu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OQU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2OQU FirstGlance]. <br> | <table><tr><td colspan='2'>[[2oqu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OQU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2OQU FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=XE:XENON'>XE</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=XE:XENON'>XE</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2oqn|2oqn]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2oqn|2oqn]]</td></tr> | ||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pancreatic_elastase Pancreatic elastase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.36 3.4.21.36] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pancreatic_elastase Pancreatic elastase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.36 3.4.21.36] </span></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2oqu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oqu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2oqu RCSB], [http://www.ebi.ac.uk/pdbsum/2oqu PDBsum]</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=2oqu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oqu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2oqu RCSB], [http://www.ebi.ac.uk/pdbsum/2oqu PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/ELA1_PIG ELA1_PIG]] Acts upon elastin. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Pancreatic elastase]] | [[Category: Pancreatic elastase]] | ||
[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
[[Category: Gruner, S M | [[Category: Gruner, S M]] | ||
[[Category: Hao, Q | [[Category: Hao, Q]] | ||
[[Category: Kim, C U | [[Category: Kim, C U]] | ||
[[Category: High pressure cryocooling]] | [[Category: High pressure cryocooling]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Sad phasing]] | [[Category: Sad phasing]] | ||
[[Category: Xenon]] | [[Category: Xenon]] | ||
Revision as of 16:59, 25 December 2014
High Pressure Cryocooling of Capillary Sample Cryoprotection and Diffraction Phasing at Long WavelengthsHigh Pressure Cryocooling of Capillary Sample Cryoprotection and Diffraction Phasing at Long Wavelengths
Structural highlights
Function[ELA1_PIG] Acts upon elastin. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCrystal cryocooling is usually employed to reduce radiation damage during X-ray crystallography. Recently, a high-pressure cryocooling method has been developed which results in excellent diffraction-quality crystals without the use of penetrative cryoprotectants. Three new developments of the method are presented here: (i) Xe-He high-pressure cryocooling for Xe SAD phasing, (ii) native sulfur SAD phasing and (iii) successful cryopreservation of crystals in thick-walled capillaries without additional cryoprotectants other than the native mother liquor. These developments may be useful for structural solution of proteins without the need for selenomethionine incorporation and for high-throughput protein crystallography. High-pressure cryocooling for capillary sample cryoprotection and diffraction phasing at long wavelengths.,Kim CU, Hao Q, Gruner SM Acta Crystallogr D Biol Crystallogr. 2007 May;63(Pt 5):653-9. Epub 2007, Apr 21. PMID:17452791[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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