Heating of proteins as a means of improving crystallization: a successful case study on a highly amyloidogenic triple mutant of human transthyretin.
2007 (English)In: Acta Crystallographica. Section F: Structural Biology and Crystallization Communications, ISSN 1744-3091, Vol. 63, no Pt 8, 695-700 p.Article in journal (Refereed) Published
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.
Place, publisher, year, edition, pages
2007. Vol. 63, no Pt 8, 695-700 p.
Amyloid/*biosynthesis/genetics, Crystallization/methods, Crystallography; X-Ray, Genetic Heterogeneity, Heat, Humans, Mutation, Prealbumin/*chemistry/*genetics/isolation & purification
IdentifiersURN: urn:nbn:se:umu:diva-16830DOI: 10.1107/S1744309107033957PubMedID: 17671371OAI: oai:DiVA.org:umu-16830DiVA: diva2:156503