2qel
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(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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Revision as of 21:26, 12 November 2007
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Crystal structure of the highly amyloidogenic transthyretin mutant TTR G53S/E54D/L55S- heated protein
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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.
Disease
Known diseases associated with this structure: Amyloid neuropathy, familial, several allelic types OMIM:[176300], Amyloidosis, senile systemic OMIM:[176300], Carpal tunnel syndrome, familial OMIM:[176300], Dystransthyretinemic hyperthyroxinemia OMIM:[176300]
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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