4n5r: Difference between revisions
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== | ==Hen egg-white lysozyme phased using free-electron laser data== | ||
[[http://www.uniprot.org/uniprot/LYSC_CHICK LYSC_CHICK | <StructureSection load='4n5r' size='340' side='right'caption='[[4n5r]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4n5r]] 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=4N5R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4N5R 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]] 2.1Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DO3:10-((2R)-2-HYDROXYPROPYL)-1,4,7,10-TETRAAZACYCLODODECANE+1,4,7-TRIACETIC+ACID'>DO3</scene>, <scene name='pdbligand=GD:GADOLINIUM+ATOM'>GD</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=4n5r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n5r OCA], [https://pdbe.org/4n5r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4n5r RCSB], [https://www.ebi.ac.uk/pdbsum/4n5r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4n5r 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 determination of protein crystal structures is hampered by the need for macroscopic crystals. X-ray free-electron lasers (FELs) provide extremely intense pulses of femtosecond duration, which allow data collection from nanometre- to micrometre-sized crystals in a 'diffraction-before-destruction' approach. So far, all protein structure determinations carried out using FELs have been based on previous knowledge of related, known structures. Here we show that X-ray FEL data can be used for de novo protein structure determination, that is, without previous knowledge about the structure. Using the emerging technique of serial femtosecond crystallography, we performed single-wavelength anomalous scattering measurements on microcrystals of the well-established model system lysozyme, in complex with a lanthanide compound. Using Monte-Carlo integration, we obtained high-quality diffraction intensities from which experimental phases could be determined, resulting in an experimental electron density map good enough for automated building of the protein structure. This demonstrates the feasibility of determining novel protein structures using FELs. We anticipate that serial femtosecond crystallography will become an important tool for the structure determination of proteins that are difficult to crystallize, such as membrane proteins. | |||
De novo protein crystal structure determination from X-ray free-electron laser data.,Barends TR, Foucar L, Botha S, Doak RB, Shoeman RL, Nass K, Koglin JE, Williams GJ, Boutet S, Messerschmidt M, Schlichting I Nature. 2013 Nov 24. doi: 10.1038/nature12773. PMID:24270807<ref>PMID:24270807</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
< | </div> | ||
[[Category: | <div class="pdbe-citations 4n5r" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: Barends | ==See Also== | ||
[[Category: Botha | *[[Lysozyme 3D structures|Lysozyme 3D structures]] | ||
[[Category: Boutet | == References == | ||
[[Category: Doak | <references/> | ||
[[Category: Foucar | __TOC__ | ||
[[Category: Koglin | </StructureSection> | ||
[[Category: Messerschmidt | [[Category: Gallus gallus]] | ||
[[Category: Nass | [[Category: Large Structures]] | ||
[[Category: Schlichting | [[Category: Barends TRM]] | ||
[[Category: Shoeman | [[Category: Botha S]] | ||
[[Category: Williams | [[Category: Boutet S]] | ||
[[Category: Doak RB]] | |||
[[Category: Foucar L]] | |||
[[Category: Koglin JE]] | |||
[[Category: Messerschmidt M]] | |||
[[Category: Nass K]] | |||
[[Category: Schlichting I]] | |||
[[Category: Shoeman RL]] | |||
[[Category: Williams GJ]] | |||
Latest revision as of 13:06, 16 August 2023
Hen egg-white lysozyme phased using free-electron laser dataHen egg-white lysozyme phased using free-electron laser data
Structural highlights
FunctionLYSC_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 PubMedThe determination of protein crystal structures is hampered by the need for macroscopic crystals. X-ray free-electron lasers (FELs) provide extremely intense pulses of femtosecond duration, which allow data collection from nanometre- to micrometre-sized crystals in a 'diffraction-before-destruction' approach. So far, all protein structure determinations carried out using FELs have been based on previous knowledge of related, known structures. Here we show that X-ray FEL data can be used for de novo protein structure determination, that is, without previous knowledge about the structure. Using the emerging technique of serial femtosecond crystallography, we performed single-wavelength anomalous scattering measurements on microcrystals of the well-established model system lysozyme, in complex with a lanthanide compound. Using Monte-Carlo integration, we obtained high-quality diffraction intensities from which experimental phases could be determined, resulting in an experimental electron density map good enough for automated building of the protein structure. This demonstrates the feasibility of determining novel protein structures using FELs. We anticipate that serial femtosecond crystallography will become an important tool for the structure determination of proteins that are difficult to crystallize, such as membrane proteins. De novo protein crystal structure determination from X-ray free-electron laser data.,Barends TR, Foucar L, Botha S, Doak RB, Shoeman RL, Nass K, Koglin JE, Williams GJ, Boutet S, Messerschmidt M, Schlichting I Nature. 2013 Nov 24. doi: 10.1038/nature12773. PMID:24270807[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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