2qel: Difference between revisions

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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.

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==

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==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17671371 17671371]

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 Crystallogr Sect F Struct Biol Cryst Commun. 2007 Aug 1;63(Pt, 8):695-700. Epub 2007 Jul 21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17671371 17671371]

[[Category: Homo sapiens]]

[[Category: Single protein]]

[[Category: Karlsson, A.]]

[[Category: Sauer-Eriksson, A.E.]]

[[Category: Sauer-Eriksson, A E.]]

[[Category: beta barrel]]

[[Category: beta-slip]]

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[[Category: transport protein]]

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@@ Line 4: / Line 4: @@
 ==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==
@@ Line 10: / Line 13: @@
 ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17671371 17671371]
+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 Crystallogr Sect F Struct Biol Cryst Commun. 2007 Aug 1;63(Pt, 8):695-700. Epub 2007 Jul 21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17671371 17671371]
 [[Category: Homo sapiens]]
 [[Category: Single protein]]
 [[Category: Karlsson, A.]]
-[[Category: Sauer-Eriksson, A.E.]]
+[[Category: Sauer-Eriksson, A E.]]
 [[Category: beta barrel]]
 [[Category: beta-slip]]
@@ Line 21: / Line 24: @@
 [[Category: transport protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 13:46:34 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:38:43 2008''