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| | <StructureSection load='5a3e' size='340' side='right'caption='[[5a3e]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='5a3e' size='340' side='right'caption='[[5a3e]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5a3e]] 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=5A3E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5A3E FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5a3e]] 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=5A3E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5A3E 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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron crystallography, [[Resolution|Resolution]] 2.501Å</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=5a3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a3e OCA], [http://pdbe.org/5a3e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5a3e RCSB], [http://www.ebi.ac.uk/pdbsum/5a3e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5a3e ProSAT]</span></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=5a3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a3e OCA], [https://pdbe.org/5a3e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5a3e RCSB], [https://www.ebi.ac.uk/pdbsum/5a3e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5a3e ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == 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> | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | [[Category: Gallus gallus]] | | [[Category: Gallus gallus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lysozyme]]
| + | [[Category: Gonen T]] |
| - | [[Category: Gonen, T]] | + | [[Category: Leslie AGW]] |
| - | [[Category: Leslie, A G.W]] | + | [[Category: Nannenga BL]] |
| - | [[Category: Nannenga, B L]] | + | [[Category: Shi D]] |
| - | [[Category: Shi, D]] | + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Microed]]
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| Structural highlights
Function
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.[1]
Publication Abstract from PubMed
MicroED uses very small three-dimensional protein crystals and electron diffraction for structure determination. We present an improved data collection protocol for MicroED called 'continuous rotation'. Microcrystals are continuously rotated during data collection, yielding more accurate data. The method enables data processing with the crystallographic software tool MOSFLM, which resulted in improved resolution for the model protein lysozyme. These improvements are paving the way for the broad implementation and application of MicroED in structural biology.
High-resolution structure determination by continuous-rotation data collection in MicroED.,Nannenga BL, Shi D, Leslie AG, Gonen T Nat Methods. 2014 Aug 3. doi: 10.1038/nmeth.3043. PMID:25086503[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Maehashi K, Matano M, Irisawa T, Uchino M, Kashiwagi Y, Watanabe T. Molecular characterization of goose- and chicken-type lysozymes in emu (Dromaius novaehollandiae): evidence for extremely low lysozyme levels in emu egg white. Gene. 2012 Jan 15;492(1):244-9. doi: 10.1016/j.gene.2011.10.021. Epub 2011 Oct, 25. PMID:22044478 doi:10.1016/j.gene.2011.10.021
- ↑ Nannenga BL, Shi D, Leslie AG, Gonen T. High-resolution structure determination by continuous-rotation data collection in MicroED. Nat Methods. 2014 Aug 3. doi: 10.1038/nmeth.3043. PMID:25086503 doi:http://dx.doi.org/10.1038/nmeth.3043
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