7l84

<table><tr><td colspan='2'>[[7l84]] 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=7L84 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7L84 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=7l84 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7l84 OCA], [https://pdbe.org/7l84 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7l84 RCSB], [https://www.ebi.ac.uk/pdbsum/7l84 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7l84 ProSAT]</span></td></tr>

== 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>

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== Publication Abstract from PubMed ==

Single-wavelength anomalous diffraction (SAD) is a routine method for overcoming the phase problem when solving macromolecular structures. This technique requires the accurate measurement of intensities to determine differences between Bijvoet pairs. Although SAD experiments are commonly conducted at cryogenic temperatures to mitigate the effects of radiation damage, such temperatures can alter the conformational ensemble of the protein and may impede the merging of data from multiple crystals due to non-uniform freezing. Here, a strategy is presented to obtain high-quality data from room-temperature, single-crystal experiments. To illustrate the strengths of this approach, native SAD phasing at 6.55 keV was used to solve four structures of three model systems at 295 K. The resulting data sets allow automatic phasing and model building, and reveal alternate conformations that reflect the structure of proteins at room temperature.

Native SAD phasing at room temperature.,Greisman JB, Dalton KM, Sheehan CJ, Klureza MA, Kurinov I, Hekstra DR Acta Crystallogr D Struct Biol. 2022 Aug 1;78(Pt 8):986-996. doi:, 10.1107/S2059798322006799. Epub 2022 Jul 27. PMID:35916223<ref>PMID:35916223</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Gallus gallus]]