7xe9: Difference between revisions
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==T4 lysozyme mutant-S44C/C54T/N68C/A93C/C97A/T115C, DMSO 20%== | |||
<StructureSection load='7xe9' size='340' side='right'caption='[[7xe9]], [[Resolution|resolution]] 1.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7xe9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7XE9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XE9 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>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEZ:HEXANE-1,6-DIOL'>HEZ</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=7xe9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xe9 OCA], [https://pdbe.org/7xe9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xe9 RCSB], [https://www.ebi.ac.uk/pdbsum/7xe9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xe9 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/D9IEF7_BPT4 D9IEF7_BPT4] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Protein crystals are generally fragile and sensitive to subtle changes such as pH, ionic strength, and/or temperature in their crystallization mother liquor. Here, using T4 phage lysozyme as a model protein, the three-dimensional rigidification of protein crystals was conducted by introducing disulfide cross-links between neighboring molecules in the crystal. The effect of cross-linking on the stability of the crystals was evaluated by microscopic observation and X-ray diffraction. When soaking the obtained cross-linked crystals into a precipitant-free solution, the crystals held their shape without dissolution and diffracted to approximately 1.1 A resolution, comparable to that of the non-cross-linked crystals. Such cross-linked crystals maintained their diffraction even when immersed in other solutions with pH values from 4 to 10, indicating that the disulfide cross-linking made the packing contacts enforced and resulted in some mechanical strength in response to changes in the preservation conditions. Furthermore, the cross-linked crystals gained stability to permit soaking into solutions containing high concentrations of organic solvents. The results suggest the possibility of obtaining protein crystals for effective drug screening by introducing appropriate cross-linked disulfide bonds. | |||
Creation of Cross-Linked Crystals With Intermolecular Disulfide Bonds Connecting Symmetry-Related Molecules Allows Retention of Tertiary Structure in Different Solvent Conditions.,Hiromoto T, Ikura T, Honjo E, Blaber M, Kuroki R, Tamada T Front Mol Biosci. 2022 Jun 8;9:908394. doi: 10.3389/fmolb.2022.908394. , eCollection 2022. PMID:35755825<ref>PMID:35755825</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Hiromoto | <div class="pdbe-citations 7xe9" style="background-color:#fffaf0;"></div> | ||
[[Category: Tamada | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia virus T4]] | |||
[[Category: Large Structures]] | |||
[[Category: Hiromoto T]] | |||
[[Category: Tamada T]] | |||
Revision as of 10:16, 22 March 2023
T4 lysozyme mutant-S44C/C54T/N68C/A93C/C97A/T115C, DMSO 20%T4 lysozyme mutant-S44C/C54T/N68C/A93C/C97A/T115C, DMSO 20%
Structural highlights
FunctionPublication Abstract from PubMedProtein crystals are generally fragile and sensitive to subtle changes such as pH, ionic strength, and/or temperature in their crystallization mother liquor. Here, using T4 phage lysozyme as a model protein, the three-dimensional rigidification of protein crystals was conducted by introducing disulfide cross-links between neighboring molecules in the crystal. The effect of cross-linking on the stability of the crystals was evaluated by microscopic observation and X-ray diffraction. When soaking the obtained cross-linked crystals into a precipitant-free solution, the crystals held their shape without dissolution and diffracted to approximately 1.1 A resolution, comparable to that of the non-cross-linked crystals. Such cross-linked crystals maintained their diffraction even when immersed in other solutions with pH values from 4 to 10, indicating that the disulfide cross-linking made the packing contacts enforced and resulted in some mechanical strength in response to changes in the preservation conditions. Furthermore, the cross-linked crystals gained stability to permit soaking into solutions containing high concentrations of organic solvents. The results suggest the possibility of obtaining protein crystals for effective drug screening by introducing appropriate cross-linked disulfide bonds. Creation of Cross-Linked Crystals With Intermolecular Disulfide Bonds Connecting Symmetry-Related Molecules Allows Retention of Tertiary Structure in Different Solvent Conditions.,Hiromoto T, Ikura T, Honjo E, Blaber M, Kuroki R, Tamada T Front Mol Biosci. 2022 Jun 8;9:908394. doi: 10.3389/fmolb.2022.908394. , eCollection 2022. PMID:35755825[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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