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Heating of proteins as a means of improving crystallization: a successful case study on a highly amyloidogenic triple mutant of human transthyretin
- Source :
- Acta Crystallographica Section F Structural Biology and Crystallization Communications. 63:695-700
- Publication Year :
- 2007
- Publisher :
- International Union of Crystallography (IUCr), 2007.
-
Abstract
- 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.
- Subjects :
- Amyloid
Hot Temperature
Biophysics
macromolecular substances
Crystallography, X-Ray
medicine.disease_cause
Biochemistry
law.invention
Genetic Heterogeneity
Structural Biology
law
Genetics
medicine
Humans
Prealbumin
Crystallization
Mutation
biology
Chemistry
Condensed Matter Physics
Transport protein
Triple mutant
Transthyretin
Crystallization Communications
biology.protein
Subjects
Details
- ISSN :
- 17443091
- Volume :
- 63
- Database :
- OpenAIRE
- Journal :
- Acta Crystallographica Section F Structural Biology and Crystallization Communications
- Accession number :
- edsair.doi.dedup.....918d84ae93d4e9de4f378843d248db64