8h3w
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[8h3w]] 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=8H3W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8H3W FirstGlance]. <br> | <table><tr><td colspan='2'>[[8h3w]] 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=8H3W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8H3W FirstGlance]. <br> | ||
| - | </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=8h3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8h3w OCA], [https://pdbe.org/8h3w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8h3w RCSB], [https://www.ebi.ac.uk/pdbsum/8h3w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8h3w ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.39Å</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=8h3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8h3w OCA], [https://pdbe.org/8h3w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8h3w RCSB], [https://www.ebi.ac.uk/pdbsum/8h3w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8h3w ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == 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> | [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 == | ||
| + | High-resolution biomacromolecular structure determination is essential to better understand protein function and dynamics. Serial crystallography is an emerging structural biology technique which has fundamental limitations due to either sample volume requirements or immediate access to the competitive X-ray beamtime. Obtaining a high volume of well-diffracting, sufficient-size crystals while mitigating radiation damage remains a critical bottleneck of serial crystallography. As an alternative, we introduce the plate-reader module adapted for using a 72-well Terasaki plate for biomacromolecule structure determination at a convenience of a home X-ray source. We also present the first ambient temperature lysozyme structure determined at the Turkish light source (Turkish DeLight). The complete dataset was collected in 18.5 min with resolution extending to 2.39 A and 100% completeness. Combined with our previous cryogenic structure (PDB ID: 7Y6A), the ambient temperature structure provides invaluable information about the structural dynamics of the lysozyme. Turkish DeLight provides robust and rapid ambient temperature biomacromolecular structure determination with limited radiation damage. | ||
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| + | Rapid and efficient ambient temperature X-ray crystal structure determination at Turkish Light Source.,Gul M, Ayan E, Destan E, Johnson JA, Shafiei A, Kepceoglu A, Yilmaz M, Ertem FB, Yapici I, Tosun B, Baldir N, Tokay N, Nergiz Z, Karakadioglu G, Paydos SS, Kulakman C, Ferah CK, Guven O, Atalay N, Akcan EK, Cetinok H, Arslan NE, Sabanoglu K, Asci B, Tavli S, Gumusboga H, Altuntas S, Otsuka M, Fujita M, Teki N S, Ci Ftci H, Durdagi S, Karaca E, Kaplan Turkoz B, Kabasakal BV, Kati A, DeMi Rci H Sci Rep. 2023 May 19;13(1):8123. doi: 10.1038/s41598-023-33989-0. PMID:37208392<ref>PMID:37208392</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 8h3w" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Lysozyme 3D structures|Lysozyme 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Crystal structure of chicken egg lysozyme at ambient temperature
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