3ih3: Difference between revisions
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==TM1030 crystallized at 310K== | ==TM1030 crystallized at 310K== | ||
<StructureSection load='3ih3' size='340' side='right' caption='[[3ih3]], [[Resolution|resolution]] 2.35Å' scene=''> | <StructureSection load='3ih3' size='340' side='right'caption='[[3ih3]], [[Resolution|resolution]] 2.35Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3ih3]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3ih3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IH3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IH3 FirstGlance]. <br> | ||
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ih2|3ih2]], [[3ih4|3ih4]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3ih2|3ih2]], [[3ih4|3ih4]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TM1030, TM_1030 ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TM1030, TM_1030 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 ATCC 43589])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ih3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ih3 OCA], [https://pdbe.org/3ih3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ih3 RCSB], [https://www.ebi.ac.uk/pdbsum/3ih3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ih3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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</div> | </div> | ||
<div class="pdbe-citations 3ih3" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 3ih3" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Tetracycline repressor protein 3D structures|Tetracycline repressor protein 3D structures]] | |||
*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Atcc 43589]] | [[Category: Atcc 43589]] | ||
[[Category: Large Structures]] | |||
[[Category: Bujacz, G]] | [[Category: Bujacz, G]] | ||
[[Category: Chruszcz, M]] | [[Category: Chruszcz, M]] | ||
Revision as of 12:55, 13 April 2022
TM1030 crystallized at 310KTM1030 crystallized at 310K
Structural highlights
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 PubMedTranscriptional regulator protein TM1030 from the hyperthermophile Thermotoga maritima, as well as its complex with DNA, was crystallized at a wide range of temperatures. Crystallization plates were incubated at 4, 20, 37 and 50 degrees C over 3 weeks. The best crystals of TM1030 in complex with DNA were obtained at 4, 20 and 37 degrees C, while TM1030 alone crystallized almost equally well in all temperatures. The crystals grown at different temperatures were used for X-ray diffraction experiments and their structures were compared. Surprisingly, the models of TM1030 obtained from crystals grown at different temperatures are similar in quality. While there are some examples of structures of proteins grown at elevated temperatures in the PDB, these temperatures appear to be underrepresented. Our studies show that crystals of some proteins may be grown and are stable at broad range of temperatures. We suggest that crystallization experiments at elevated temperatures could be used as a standard part of the crystallization protocol. 'Hot' macromolecular crystals.,Koclega KD, Chruszcz M, Zimmerman MD, Bujacz G, Minor W Cryst Growth Des. 2009 Dec 18;10(2):580. PMID:20161694[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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