9cbe
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of a type III antifreeze protein isoform HPLC12 re-refined using standard protocols== | |
| + | <StructureSection load='9cbe' size='340' side='right'caption='[[9cbe]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[9cbe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Zoarces_americanus Zoarces americanus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9CBE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9CBE 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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9cbe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9cbe OCA], [https://pdbe.org/9cbe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9cbe RCSB], [https://www.ebi.ac.uk/pdbsum/9cbe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9cbe ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ANP12_ZOAAM ANP12_ZOAAM] Contributes to protect fish blood from freezing at subzero sea water temperatures. Lowers the blood freezing point. Binds to nascent ice crystals and prevents further growth. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The manuscript ;Modeling a unit cell: crystallographic refinement procedure using the biomolecular MD simulation platform Amber' presents a novel protein structure refinement method claimed to offer improvements over traditional techniques like Refmac5 and Phenix. Our re-evaluation suggests that while the new method provides improvements, traditional methods achieve comparable results with less computational effort. | ||
| - | + | In some cases more complicated approaches to refinement of macromolecular structures are not necessary.,Dauter Z, Wlodawer A IUCrJ. 2024 Jul 1;11(Pt 4):643-644. doi: 10.1107/S2052252524005803. PMID:38958017<ref>PMID:38958017</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Dauter | + | <div class="pdbe-citations 9cbe" style="background-color:#fffaf0;"></div> |
| - | [[Category: Wlodawer | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Zoarces americanus]] | ||
| + | [[Category: Dauter Z]] | ||
| + | [[Category: Wlodawer A]] | ||
Current revision
Structure of a type III antifreeze protein isoform HPLC12 re-refined using standard protocols
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