2oqn: Difference between revisions

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[[Image:2oqn.jpg|left|200px]]


{{Structure
==High Pressure Cryocooling of Capillary Sample Cryoprotection and Diffraction Phasing at Long Wavelengths==
|PDB= 2oqn |SIZE=350|CAPTION= <scene name='initialview01'>2oqn</scene>, resolution 1.90&Aring;
<StructureSection load='2oqn' size='340' side='right'caption='[[2oqn]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=TAR:D(-)-TARTARIC+ACID'>TAR</scene>
<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>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
|GENE=  
<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>
|DOMAIN=
<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>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2oqn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oqn OCA], [http://www.ebi.ac.uk/pdbsum/2oqn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2oqn RCSB]</span>
== 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 ==
'''High Pressure Cryocooling of Capillary Sample Cryoprotection and Diffraction Phasing at Long Wavelengths'''
[[Image:Consurf_key_small.gif|200px|right]]
 
Check<jmol>
 
  <jmolCheckbox>
==Overview==
    <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.
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.


==About this Structure==
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>
2OQN is a [[Single protein]] structure of sequence from [http://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].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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:[http://www.ncbi.nlm.nih.gov/pubmed/17452791 17452791]
</div>
[[Category: Single protein]]
<div class="pdbe-citations 2oqn" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thaumatococcus daniellii]]
[[Category: Thaumatococcus daniellii]]
[[Category: Gruner, S M.]]
[[Category: Gruner SM]]
[[Category: Hao, Q.]]
[[Category: Hao Q]]
[[Category: Kim, C U.]]
[[Category: Kim CU]]
[[Category: capillary cryoprotection]]
[[Category: high pressure cryocooling]]
[[Category: sulfur sad phasing]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:21:43 2008''

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

2oqn is a 1 chain structure with sequence from Thaumatococcus daniellii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

THM1_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 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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Kim CU, Hao Q, Gruner SM. High-pressure cryocooling for capillary sample cryoprotection and diffraction phasing at long wavelengths. Acta Crystallogr D Biol Crystallogr. 2007 May;63(Pt 5):653-9. Epub 2007, Apr 21. PMID:17452791 doi:10.1107/S0907444907011924

2oqn, resolution 1.90Å

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