8f2g: Difference between revisions

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-'''Unreleased structure'''
-The entry 8f2g is ON HOLD
+==Crystal structure of Hen Egg White Lysozyme at 0.44 GPa==
+<StructureSection load='8f2g' size='340' side='right'caption='[[8f2g]], [[Resolution|resolution]] 1.84&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[8f2g]] 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=8F2G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8F2G 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]] 1.84&#8491;</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=8f2g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8f2g OCA], [https://pdbe.org/8f2g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8f2g RCSB], [https://www.ebi.ac.uk/pdbsum/8f2g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8f2g 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 ==
+A new high-pressure single-crystal diffraction setup has been designed and implemented at the Australian Synchrotron for collecting molecular and protein crystal structures. The setup incorporates a modified micro-Merrill-Bassett cell and holder designed specifically to fit onto the horizontal air-bearing goniometer, allowing high-pressure diffraction measurements to be collected with little to no modification of the beamline setup compared with ambient data collections. Compression data for the amino acid, L-threonine, and the protein, hen egg-white lysozyme, were collected, showcasing the capabilities of the setup.
-Authors:
+High-pressure single-crystal diffraction at the Australian Synchrotron.,Boer SA, Price JR, Riboldi-Tunnicliffe A, Williamson R, Rostan R, Summers A, Turner GF, Jones I, Bond CS, Vrielink A, Marshall AC, Hitchings J, Moggach SA J Synchrotron Radiat. 2023 Jul 1;30(Pt 4):841-846. doi: , 10.1107/S160057752300406X. Epub 2023 Jun 15. PMID:37318368<ref>PMID:37318368</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 8f2g" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Lysozyme 3D structures|Lysozyme 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Gallus gallus]]
+[[Category: Large Structures]]
+[[Category: Boer SA]]
+[[Category: Bond CS]]
+[[Category: Marshall AC]]
+[[Category: Moggach SA]]
+[[Category: Turner G]]
+[[Category: Vrielink A]]