5t8b
From Proteopedia
(Difference between revisions)
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<StructureSection load='5t8b' size='340' side='right'caption='[[5t8b]], [[Resolution|resolution]] 1.50Å' scene=''> | <StructureSection load='5t8b' size='340' side='right'caption='[[5t8b]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5t8b]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[5t8b]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Legionella_pneumophila Legionella pneumophila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T8B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5T8B FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5t8b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t8b OCA], [https://pdbe.org/5t8b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5t8b RCSB], [https://www.ebi.ac.uk/pdbsum/5t8b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5t8b ProSAT]</span></td></tr> |
</table> | </table> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | High-pressure cryocooling (HPC) has been developed as a technique for reducing the damage that frequently occurs when macromolecular crystals are cryocooled at ambient pressure. Crystals are typically pressurized at around 200 MPa and then cooled to liquid nitrogen temperature under pressure; this process reduces the need for penetrating cryoprotectants, as well as the damage due to cryocooling, but does not improve the diffraction quality of the as-grown crystals. Here it is reported that HPC using a pressure above 300 MPa can reduce lattice disorder, in the form of high mosaicity and/or nonmerohedral twinning, in crystals of three different proteins, namely human glutaminase C, the GTP pyrophosphokinase YjbM and the uncharacterized protein lpg1496. Pressure lower than 250 MPa does not induce this transformation, even with a prolonged pressurization time. These results indicate that HPC at elevated pressures can be a useful tool for improving crystal packing and hence the quality of the diffraction data collected from pressurized crystals. | ||
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| - | Reduction of lattice disorder in protein crystals by high-pressure cryocooling.,Huang Q, Gruner SM, Kim CU, Mao Y, Wu X, Szebenyi DM J Appl Crystallogr. 2016 Feb 1;49(Pt 1):149-157. eCollection 2016 Feb 1. PMID:26937238<ref>PMID:26937238</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 5t8b" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Atcc 33152]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Legionella pneumophila]] |
| - | [[Category: | + | [[Category: Huang Q]] |
| - | [[Category: | + | [[Category: Szebenyi D]] |
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| - | + | ||
Current revision
Crystal structure of lpg1496 under 350 MPa
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