1h96: Difference between revisions

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-[[Image:1h96.png|left|200px]]
+==RECOMBINANT MOUSE L-CHAIN FERRITIN==
+<StructureSection load='1h96' size='340' side='right' caption='[[1h96]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1h96]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H96 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1H96 FirstGlance]. <br>
+</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>
+<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=1h96 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h96 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1h96 RCSB], [http://www.ebi.ac.uk/pdbsum/1h96 PDBsum]</span></td></tr>
+<table>
+== 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/h9/1h96_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/chain_selection.php?pdb_ID=2ata ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Cubic F432 crystals of recombinant mouse L-chain apoferritin were obtained by the hanging-drop technique with ammonium sulfate and cadmium sulfate as precipitants. The structure was refined to 2.1 and 1.6 A resolution from data obtained at room temperature and under cryogenic conditions, respectively. The structure of an eight-amino-acid loop insertion in the mouse sequence is found to be highly disordered both at room temperature and at low temperature.
-{{STRUCTURE_1h96|  PDB=1h96  |  SCENE=  }}
+Structure of mouse L-chain ferritin at 1.6 A resolution.,Granier T, Gallois B, Langlois d'Estaintot B, Dautant A, Chevalier JM, Mellado JM, Beaumont C, Santambrogio P, Arosio P, Precigoux G Acta Crystallogr D Biol Crystallogr. 2001 Nov;57(Pt 11):1491-7. Epub 2001, Oct 25. PMID:11679711<ref>PMID:11679711</ref>
-===RECOMBINANT MOUSE L-CHAIN FERRITIN===
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-{{ABSTRACT_PUBMED_11679711}}
-==About this Structure==
-[[1h96]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H96 OCA].
 ==See Also==
 *[[Ferritin|Ferritin]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:011679711</ref><references group="xtra"/>
+__TOC__
+</StructureSection>
 [[Category: Mus musculus]]
 [[Category: Arosio, P.]]