2qel
From Proteopedia
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| , resolution 2.290Å | |||||||
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| Gene: | TTR, PALB (Homo sapiens) | ||||||
| Related: | 1g1o
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Crystallogr Sect F Struct Biol Cryst Commun. 2007 Aug 1;63(Pt, 8):695-700. Epub 2007 Jul 21. PMID:17671371
Page seeded by OCA on Mon Mar 31 04:48:21 2008
