NDLI: SOn-column Protein Refolding for Crystallization

Content Provider	Springer Nature Link
Author	Oganesyan, Natalia Kim, Sung Hou Kim, Rosalind
Copyright Year	2005
Abstract	One major bottleneck in protein production in Escherichia coli for structural genomics projects is the formation of insoluble protein aggregates (inclusion bodies). The efficient refolding of proteins from inclusion bodies is becoming an important tool that can provide soluble native proteins for structural and functional studies. Here we report an on-column refolding method established at the Berkeley Structural Genomics Center (BSGC). Our method is a combination of an ‘artificial chaperone-assisted refolding’ method previously proposed and affinity chromatography to take advantage of a chromatographic step: less time-consuming, no filtration or concentration, with the additional benefit of protein purification. It can be easily automated and formatted for high-throughput process.
Starting Page	177
Ending Page	182
Page Count	6
File Format	PDF
ISSN	1345711X
Journal	Journal of Structural and Functional Genomics
Volume Number	6
Issue Number	2-3
e-ISSN	15700267
Language	English
Publisher	Kluwer Academic Publishers
Publisher Date	2005-01-01
Publisher Place	Dordrecht
Access Restriction	Subscribed
Subject Keyword	crystallization recombinant proteins refolding Human Genetics Bioinformatics Microbial Genetics and Genomics Plant Genetics & Genomics Animal Genetics and Genomics Biochemistry
Content Type	Text
Resource Type	Article
Subject	Genetics Structural Biology Biochemistry

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