6jxp: Difference between revisions

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<StructureSection load='6jxp' size='340' side='right'caption='[[6jxp]], [[Resolution|resolution]] 1.56&Aring;' scene=''>
<StructureSection load='6jxp' size='340' side='right'caption='[[6jxp]], [[Resolution|resolution]] 1.56&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6jxp]] 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=6JXP OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6JXP FirstGlance]. <br>
<table><tr><td colspan='2'>[[6jxp]] 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=6JXP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JXP FirstGlance]. <br>
</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></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]] 1.56&#8491;</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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=6jxp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jxp OCA], [http://pdbe.org/6jxp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6jxp RCSB], [http://www.ebi.ac.uk/pdbsum/6jxp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6jxp 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=6jxp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jxp OCA], [https://pdbe.org/6jxp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jxp RCSB], [https://www.ebi.ac.uk/pdbsum/6jxp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jxp 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: Nam KH]]
[[Category: Nam, K H]]
[[Category: Hydrolase]]
[[Category: Lcp]]
[[Category: Serial crystallography]]

Latest revision as of 13:04, 6 September 2023

Room temperature structure of lysozyme delivered in LCP by serial millisecond crystallographyRoom temperature structure of lysozyme delivered in LCP by serial millisecond crystallography

Structural highlights

6jxp is a 1 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.56Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

Sample delivery using injectors is widely used in serial crystallography (SX) and has significantly contributed to the determination of crystal structures at room temperature. However, sophisticated injector nozzle fabrication methods and sample delivery operations have made it difficult for ordinary users to access the SX research. Herein, a simple and easily accessible sample delivery method for SX experiments is introduced, that uses a viscous medium, commercially available syringe and syringe pump. The syringe containing the lysozyme crystals embedded in lipidic cubic phase (LCP) or polyacrylamide (PAM) delivery media was connected to a needle having an inner diameter of 168 microm, after which it was installed on a syringe pump. By driving the syringe pump, the syringe plunger was pushed and the crystal sample was delivered to the X-ray beam position in a stable manner. Using this system, the room-temperature crystal structures of lysozyme embedded in LCP and PAM at 1.56 A and 1.75 A, respectively, were determined. This straightforward syringe pump-based sample delivery system can be utilized in SX.

Sample delivery using viscous media, a syringe and a syringe pump for serial crystallography.,Park SY, Nam KH J Synchrotron Radiat. 2019 Sep 1;26(Pt 5):1815-1819. doi:, 10.1107/S160057751900897X. Epub 2019 Aug 15. PMID:31490174[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. 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
  2. Park SY, Nam KH. Sample delivery using viscous media, a syringe and a syringe pump for serial crystallography. J Synchrotron Radiat. 2019 Sep 1;26(Pt 5):1815-1819. doi:, 10.1107/S160057751900897X. Epub 2019 Aug 15. PMID:31490174 doi:http://dx.doi.org/10.1107/S160057751900897X

6jxp, resolution 1.56Å

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