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| | ==Mitigation of X-ray damage in macromolecular crystallography by submicrometer line focusing; total dose 1.32 x 10e+12 X-ray photons== | | ==Mitigation of X-ray damage in macromolecular crystallography by submicrometer line focusing; total dose 1.32 x 10e+12 X-ray photons== |
| - | <StructureSection load='4htn' size='340' side='right' caption='[[4htn]], [[Resolution|resolution]] 1.30Å' scene=''> | + | <StructureSection load='4htn' size='340' side='right'caption='[[4htn]], [[Resolution|resolution]] 1.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4htn]] 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=4HTN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HTN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4htn]] 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=4HTN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HTN 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>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4htk|4htk]], [[4htq|4htq]]</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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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'>[https://proteopedia.org/fgij/fg.htm?mol=4htn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4htn OCA], [https://pdbe.org/4htn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4htn RCSB], [https://www.ebi.ac.uk/pdbsum/4htn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4htn ProSAT]</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=4htn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4htn OCA], [http://pdbe.org/4htn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4htn RCSB], [http://www.ebi.ac.uk/pdbsum/4htn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4htn 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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| | </StructureSection> | | </StructureSection> |
| | [[Category: Gallus gallus]] | | [[Category: Gallus gallus]] |
| - | [[Category: Lysozyme]] | + | [[Category: Large Structures]] |
| - | [[Category: Alkire, R W]] | + | [[Category: Alkire RW]] |
| - | [[Category: Duke, N E.C]] | + | [[Category: Duke NEC]] |
| - | [[Category: Finfrock, Y Z]] | + | [[Category: Finfrock YZ]] |
| - | [[Category: Joachimiak, A]] | + | [[Category: Joachimiak A]] |
| - | [[Category: Lazarski, K]] | + | [[Category: Lazarski K]] |
| - | [[Category: Stern, E A]] | + | [[Category: Stern EA]] |
| - | [[Category: Glycosidase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: O-glycosyl]]
| + | |
| 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
Reported here are measurements of the penetration depth and spatial distribution of photoelectron (PE) damage excited by 18.6 keV X-ray photons in a lysozyme crystal with a vertical submicrometre line-focus beam of 0.7 microm full-width half-maximum (FWHM). The experimental results determined that the penetration depth of PEs is 5 +/- 0.5 microm with a monotonically decreasing spatial distribution shape, resulting in mitigation of diffraction signal damage. This does not agree with previous theoretical predication that the mitigation of damage requires a peak of damage outside the focus. A new improved calculation provides some qualitative agreement with the experimental results, but significant errors still remain. The mitigation of radiation damage by line focusing was measured experimentally by comparing the damage in the X-ray-irradiated regions of the submicrometre focus with the large-beam case under conditions of equal exposure and equal volumes of the protein crystal, and a mitigation factor of 4.4 +/- 0.4 was determined. The mitigation of radiation damage is caused by spatial separation of the dominant PE radiation-damage component from the crystal region of the line-focus beam that contributes the diffraction signal. The diffraction signal is generated by coherent scattering of incident X-rays (which introduces no damage), while the overwhelming proportion of damage is caused by PE emission as X-ray photons are absorbed.
Mitigation of X-ray damage in macromolecular crystallography by submicrometre line focusing.,Finfrock YZ, Stern EA, Alkire RW, Kas JJ, Evans-Lutterodt K, Stein A, Duke N, Lazarski K, Joachimiak A Acta Crystallogr D Biol Crystallogr. 2013 Aug;69(Pt 8):1463-9. doi:, 10.1107/S0907444913009335. Epub 2013 Jul 17. PMID:23897469[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
- ↑ Finfrock YZ, Stern EA, Alkire RW, Kas JJ, Evans-Lutterodt K, Stein A, Duke N, Lazarski K, Joachimiak A. Mitigation of X-ray damage in macromolecular crystallography by submicrometre line focusing. Acta Crystallogr D Biol Crystallogr. 2013 Aug;69(Pt 8):1463-9. doi:, 10.1107/S0907444913009335. Epub 2013 Jul 17. PMID:23897469 doi:10.1107/S0907444913009335
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