2qel: Difference between revisions

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New page: left|200px<br /> <applet load="2qel" size="450" color="white" frame="true" align="right" spinBox="true" caption="2qel, resolution 2.290Å" /> '''Crystal structure ...
 
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[[Image:2qel.gif|left|200px]]<br />
[[Image:2qel.jpg|left|200px]]<br /><applet load="2qel" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="2qel" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="2qel, resolution 2.290&Aring;" />
caption="2qel, resolution 2.290&Aring;" />
'''Crystal structure of the highly amyloidogenic transthyretin mutant TTR G53S/E54D/L55S- heated protein'''<br />
'''Crystal structure of the highly amyloidogenic transthyretin mutant TTR G53S/E54D/L55S- heated protein'''<br />
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==Overview==
==Overview==
The use of high temperatures in the purification procedures of heat-stable, proteins is a well established technique. Recently, rapid pre-heat, treatment of protein samples prior to crystallization trials was described, as a final polishing step to improve the diffraction properties of, crystals [Pusey et al. (2005), Prog. Biophys. Mol. Biol. 88, 359-386]. The, present study demonstrates that extended high-temperature incubation (328, K for 48 h) of the highly amyloidogenic transthyretin mutant TTR, G53S/E54D/L55S successfully removes heterogeneities and allows the, reproducible growth of well diffracting crystals. Heat treatment might be, applied as an optimization method to other cases in which the, protein/biomolecule fails to form diffracting crystals.
The use of high temperatures in the purification procedures of heat-stable, proteins is a well established technique. Recently, rapid pre-heat, treatment of protein samples prior to crystallization trials was described, as a final polishing step to improve the diffraction properties of, crystals [Pusey et al. (2005), Prog. Biophys. Mol. Biol. 88, 359-386]. The, present study demonstrates that extended high-temperature incubation (328, K for 48 h) of the highly amyloidogenic transthyretin mutant TTR, G53S/E54D/L55S successfully removes heterogeneities and allows the, reproducible growth of well diffracting crystals. Heat treatment might be, applied as an optimization method to other cases in which the, protein/biomolecule fails to form diffracting crystals.
==Disease==
Known diseases associated with this structure: Amyloid neuropathy, familial, several allelic types OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=176300 176300]], Amyloidosis, senile systemic OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=176300 176300]], Carpal tunnel syndrome, familial OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=176300 176300]], Dystransthyretinemic hyperthyroxinemia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=176300 176300]]


==About this Structure==
==About this Structure==
2QEL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2QEL OCA].  
2QEL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QEL OCA].  


==Reference==
==Reference==
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[[Category: transport protein]]
[[Category: transport protein]]


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