2qel: Difference between revisions

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[[Image:2qel.jpg|left|200px]]
{{Seed}}
[[Image:2qel.png|left|200px]]


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{{STRUCTURE_2qel|  PDB=2qel  |  SCENE=  }}  
{{STRUCTURE_2qel|  PDB=2qel  |  SCENE=  }}  


'''Crystal structure of the highly amyloidogenic transthyretin mutant TTR G53S/E54D/L55S- heated protein'''
===Crystal structure of the highly amyloidogenic transthyretin mutant TTR G53S/E54D/L55S- heated protein===




==Overview==
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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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{{ABSTRACT_PUBMED_17671371}}


==About this Structure==
==About this Structure==
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==Reference==
==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 Crystallogr Sect F Struct Biol Cryst Commun. 2007 Aug 1;63(Pt, 8):695-700. Epub 2007 Jul 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/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://www.ncbi.nlm.nih.gov/pubmed/17671371 17671371]
The beta-slip: a novel concept in transthyretin amyloidosis., Eneqvist T, Andersson K, Olofsson A, Lundgren E, Sauer-Eriksson AE, Mol Cell. 2000 Nov;6(5):1207-18. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11106758 11106758]
A comparative analysis of 23 structures of the amyloidogenic protein transthyretin., Hornberg A, Eneqvist T, Olofsson A, Lundgren E, Sauer-Eriksson AE, J Mol Biol. 2000 Sep 22;302(3):649-69. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10986125 10986125]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Protein heating]]
[[Category: Protein heating]]
[[Category: Transport protein]]
[[Category: Transport protein]]
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Revision as of 20:58, 28 July 2008

File:2qel.png

Template:STRUCTURE 2qel

Crystal structure of the highly amyloidogenic transthyretin mutant TTR G53S/E54D/L55S- heated protein

Template:ABSTRACT PUBMED 17671371

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 Crystallogr Sect F Struct Biol Cryst Commun. 2007 Aug 1;63(Pt, 8):695-700. Epub 2007 Jul 21. PMID:17671371

The beta-slip: a novel concept in transthyretin amyloidosis., Eneqvist T, Andersson K, Olofsson A, Lundgren E, Sauer-Eriksson AE, Mol Cell. 2000 Nov;6(5):1207-18. PMID:11106758

A comparative analysis of 23 structures of the amyloidogenic protein transthyretin., Hornberg A, Eneqvist T, Olofsson A, Lundgren E, Sauer-Eriksson AE, J Mol Biol. 2000 Sep 22;302(3):649-69. PMID:10986125

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