2oqn: Difference between revisions
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< | ==High Pressure Cryocooling of Capillary Sample Cryoprotection and Diffraction Phasing at Long Wavelengths== | ||
<StructureSection load='2oqn' size='340' side='right'caption='[[2oqn]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2oqn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thaumatococcus_daniellii Thaumatococcus daniellii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OQN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OQN FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TAR:D(-)-TARTARIC+ACID'>TAR</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=2oqn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oqn OCA], [https://pdbe.org/2oqn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2oqn RCSB], [https://www.ebi.ac.uk/pdbsum/2oqn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2oqn ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/THM1_THADA THM1_THADA] Taste-modifying protein; intensely sweet-tasting. It is 100000 times sweeter than sucrose on a molar basis. | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oq/2oqn_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2oqn ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Crystal 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<ref>PMID:17452791</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2oqn" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Large Structures]] | ||
== | |||
[[Category: | |||
[[Category: Thaumatococcus daniellii]] | [[Category: Thaumatococcus daniellii]] | ||
[[Category: Gruner | [[Category: Gruner SM]] | ||
[[Category: Hao | [[Category: Hao Q]] | ||
[[Category: Kim | [[Category: Kim CU]] | ||
Latest revision as of 13:47, 30 August 2023
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
FunctionTHM1_THADA Taste-modifying protein; intensely sweet-tasting. It is 100000 times sweeter than sucrose on a molar basis. 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. References
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