9h3e
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Hen egg white lysozyme crystallization and structure determination at room temperature in the CrystalChip== | |
| + | <StructureSection load='9h3e' size='340' side='right'caption='[[9h3e]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[9h3e]] 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=9H3E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9H3E 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]] 1.5Å</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>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=9h3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9h3e OCA], [https://pdbe.org/9h3e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9h3e RCSB], [https://www.ebi.ac.uk/pdbsum/9h3e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9h3e 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 == | ||
| + | The production of high-quality crystals is a key step in crystallography in general, but control of crystallization conditions is even more crucial in serial crystallography, which requires sets of crystals homogeneous in size and diffraction properties. This protocol describes the implementation of a simple and user-friendly microfluidic device that allows both the production of crystals by the counter-diffusion method and their in situ analysis by serial crystallography. As an illustration, the whole procedure is used to determine the crystal structure of three proteins from data collected at room temperature at a synchrotron radiation source. | ||
| - | + | Protein crystallization and structure determination at room temperature in the CrystalChip.,Pachl P, Coudray L, Vincent R, Nilles L, Scheer H, Ritzenthaler C, Fejfarova A, Rezacova P, Engilberge S, Sauter C FEBS Open Bio. 2024 Nov 21. doi: 10.1002/2211-5463.13932. PMID:39572886<ref>PMID:39572886</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 9h3e" style="background-color:#fffaf0;"></div> |
| - | [[Category: Coudray | + | == References == |
| - | [[Category: | + | <references/> |
| - | [[Category: Sauter | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Gallus gallus]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Coudray L]] | ||
| + | [[Category: Pachl P]] | ||
| + | [[Category: Sauter C]] | ||
| + | [[Category: VIncent R]] | ||
Current revision
Hen egg white lysozyme crystallization and structure determination at room temperature in the CrystalChip
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