6s2n

<table><tr><td colspan='2'>[[6s2n]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6S2N OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6S2N FirstGlance]. <br>

</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6s2n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6s2n OCA], [http://pdbe.org/6s2n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6s2n RCSB], [http://www.ebi.ac.uk/pdbsum/6s2n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6s2n ProSAT]</span></td></tr>

== Function ==

[[http://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 ==

Serial X-ray crystallography at free-electron lasers allows to solve biomolecular structures from sub-micron-sized crystals. However, beam time at these facilities is scarce, and involved sample delivery techniques are required. On the other hand, rotation electron diffraction (MicroED) has shown great potential as an alternative means for protein nano-crystallography. Here, we present a method for serial electron diffraction of protein nanocrystals combining the benefits of both approaches. In a scanning transmission electron microscope, crystals randomly dispersed on a sample grid are automatically mapped, and a diffraction pattern at fixed orientation is recorded from each at a high acquisition rate. Dose fractionation ensures minimal radiation damage effects. We demonstrate the method by solving the structure of granulovirus occlusion bodies and lysozyme to resolutions of 1.55 A and 1.80 A, respectively. Our method promises to provide rapid structure determination for many classes of materials with minimal sample consumption, using readily available instrumentation.

Serial protein crystallography in an electron microscope.,Bucker R, Hogan-Lamarre P, Mehrabi P, Schulz EC, Bultema LA, Gevorkov Y, Brehm W, Yefanov O, Oberthur D, Kassier GH, Dwayne Miller RJ Nat Commun. 2020 Feb 21;11(1):996. doi: 10.1038/s41467-020-14793-0. PMID:32081905<ref>PMID:32081905</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]]

[[Category: Buecker, R]]

[[Category: Hogan-Lamarre, P]]

[[Category: Mehrabi, P]]

[[Category: Schulz, E C]]

[[Category: Serial crystallography]]