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Published online before print July 27, 2007, 10.1110/ps.072931407
Protein Science (2007), 16:2023-2029. Published by Cold Spring Harbor Laboratory Press. Copyright © 2007 The Protein Society
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Production of selenomethionyl-derivatized proteins in baculovirus-infected insect cells

Ciarán N. Cronin1, Kheng B. Lim, and Joe Rogers2

Takeda San Diego, San Diego, California 92121, USA

(RECEIVED April 6, 2007; FINAL REVISION June 1, 2007; ACCEPTED June 5, 2007)

A protocol is described for the production of both intracellularly expressed and secreted selenomethionyl-derivatized recombinant proteins in baculovirus-infected insect cells. The method results in the production of recombinant soluble proteins with an SeMet occupancy of ~75% and with a recovery of ~20% that of native protein expression. The method is independent of the percentage methionine content of the protein and is reliable and consistent. Similar results are obtained using either Spodoptera frugiperda Sf9 or Trichoplusia ni High Five insect cells as the expression host, and when cultures are grown in either shake flasks or in Wave BioReactors.

Keywords: selenomethionine; baculovirus; insect cells; MAD phasing; multiwavelength anomalous diffraction


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 Brief Funct Genomic ProteomicHome page
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Brief Funct Genomic Proteomic, July 16, 2008; (2008) eln034v1.
[Abstract] [Full Text] [PDF]


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