SOn-column Protein Refolding for Crystallization |
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| Authors: | Natalia Oganesyan Sung-Hou Kim Rosalind Kim |
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| Institution: | (1) Berkeley Structural Genomics Center, Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA;(2) Department of Chemistry, University of California, Berkeley, California 94720, USA |
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| 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. |
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| Keywords: | crystallization recombinant proteins refolding |
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