2qel
From Proteopedia
(New page: 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. | + | [[Image:2qel.jpg|left|200px]]<br /><applet load="2qel" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2qel" size=" | + | |
caption="2qel, resolution 2.290Å" /> | caption="2qel, resolution 2.290Å" /> | ||
'''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. | ||
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| - | ==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:// | + | 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]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 13:46:34 2008'' |
Revision as of 11:46, 23 January 2008
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Crystal structure of the highly amyloidogenic transthyretin mutant TTR G53S/E54D/L55S- heated protein
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.
About this Structure
2QEL is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Heating of proteins as a means of improving crystallization: a successful case study on a highly amyloidogenic triple mutant of human transthyretin., Karlsson A, Sauer-Eriksson AE, Acta Crystallograph Sect F Struct Biol Cryst Commun. 2007 Aug 1;63(Pt, 8):695-700. Epub 2007 Jul 21. PMID:17671371
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