6h3b
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Lysozyme: Machining protein microcrystals for structure determination by electron diffraction== | |
| + | <StructureSection load='6h3b' size='340' side='right' caption='[[6h3b]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6h3b]] 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=6H3B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6H3B FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6h3b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6h3b OCA], [http://pdbe.org/6h3b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6h3b RCSB], [http://www.ebi.ac.uk/pdbsum/6h3b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6h3b ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == 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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | We demonstrate that ion-beam milling of frozen, hydrated protein crystals to thin lamella preserves the crystal lattice to near-atomic resolution. This provides a vehicle for protein structure determination, bridging the crystal size gap between the nanometer scale of conventional electron diffraction and micron scale of synchrotron microfocus beamlines. The demonstration that atomic information can be retained suggests that milling could provide such detail on sections cut from vitrified cells. | ||
| - | + | Machining protein microcrystals for structure determination by electron diffraction.,Duyvesteyn HME, Kotecha A, Ginn HM, Hecksel CW, Beale EV, de Haas F, Evans G, Zhang P, Chiu W, Stuart DI Proc Natl Acad Sci U S A. 2018 Aug 31. pii: 1809978115. doi:, 10.1073/pnas.1809978115. PMID:30171169<ref>PMID:30171169</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Duyvesteyn, H | + | <div class="pdbe-citations 6h3b" style="background-color:#fffaf0;"></div> |
| - | [[Category: Ginn, H | + | == References == |
| - | [[Category: Stuart, D | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Gallus gallus]] | ||
| + | [[Category: Lysozyme]] | ||
| + | [[Category: Duyvesteyn, H M.E]] | ||
| + | [[Category: Ginn, H M]] | ||
| + | [[Category: Stuart, D I]] | ||
| + | [[Category: Hydrolase]] | ||
Revision as of 07:41, 12 September 2018
Lysozyme: Machining protein microcrystals for structure determination by electron diffraction
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