6qqf: Difference between revisions

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-'''Unreleased structure'''
-The entry 6qqf is ON HOLD  until Paper Publication
+==Room temperature structure of Hen Egg White Lysozyme recorded after an accumulated dose of 100 kGy==
+<StructureSection load='6qqf' size='340' side='right'caption='[[6qqf]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6qqf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QQF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6QQF 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]] 1.95&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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=6qqf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qqf OCA], [https://pdbe.org/6qqf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6qqf RCSB], [https://www.ebi.ac.uk/pdbsum/6qqf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6qqf ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/LYSC_CHICK LYSC_CHICK] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has bacteriolytic activity against M.luteus.<ref>PMID:22044478</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Carrying out macromolecular crystallography (MX) experiments at cryogenic temperatures significantly slows the rate of global radiation damage, thus facilitating the solution of high-resolution crystal structures of macromolecules. However, cryo-MX experiments suffer from the early onset of so-called specific radiation damage that affects certain amino-acid residues and, in particular, the active sites of many proteins. Here, a series of MX experiments are described which suggest that specific and global radiation damage are much less decoupled at room temperature than they are at cryogenic temperatures. The results reported here demonstrate the interest in reviving the practice of collecting MX diffraction data at room temperature and allow structural biologists to favourably envisage the development of time-resolved MX experiments at synchrotron sources.
-Authors:
+Specific radiation damage is a lesser concern at room temperature.,Gotthard G, Aumonier S, De Sanctis D, Leonard G, von Stetten D, Royant A IUCrJ. 2019 Jun 12;6(Pt 4):665-680. doi: 10.1107/S205225251900616X. eCollection, 2019 Jul 1. PMID:31316810<ref>PMID:31316810</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6qqf" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Lysozyme 3D structures|Lysozyme 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Gallus gallus]]
+[[Category: Large Structures]]
+[[Category: Aumonier S]]
+[[Category: Gotthard G]]
+[[Category: Royant A]]