3ih2: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 1: Line 1:
==TM1030 crystallized at 323K==
==TM1030 crystallized at 323K==
<StructureSection load='3ih2' size='340' side='right' caption='[[3ih2]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='3ih2' size='340' side='right' caption='[[3ih2]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
Line 6: Line 7:
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ih3|3ih3]], [[3ih4|3ih4]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ih3|3ih3]], [[3ih4|3ih4]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TM1030, TM_1030 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 ATCC 43589])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TM1030, TM_1030 ([http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ih2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ih2 OCA], [http://pdbe.org/3ih2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ih2 RCSB], [http://www.ebi.ac.uk/pdbsum/3ih2 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=3ih2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ih2 OCA], [http://pdbe.org/3ih2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ih2 RCSB], [http://www.ebi.ac.uk/pdbsum/3ih2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ih2 ProSAT]</span></td></tr>
</table>
</table>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
Line 12: Line 13:
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ih/3ih2_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ih/3ih2_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>

Revision as of 12:35, 19 December 2018

TM1030 crystallized at 323KTM1030 crystallized at 323K

Structural highlights

3ih2 is a 1 chain structure with sequence from Atcc 43589. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Gene:TM1030, TM_1030 (ATCC 43589)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

Transcriptional 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.

References

  1. Koclega KD, Chruszcz M, Zimmerman MD, Bujacz G, Minor W. 'Hot' macromolecular crystals. Cryst Growth Des. 2009 Dec 18;10(2):580. PMID:20161694 doi:10.1021/cg900971h

3ih2, resolution 2.30Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA