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Functional expression of His-tagged sensory rhodopsin I in Escherichia coli
G Schmies1, I Chizhov, M Engelhard
1Max-Planck-Institut für Molekulare Physiologie, Otto-Hahn Strasse 11, D-44227, Dortmund, Germany.
FEBS Letters
|January 29, 2000
Abstract:
Sensory rhodopsin I (SRI) from Halobacterium salinarum was functionally expressed in Escherichia coli and subsequently purified to homogeneity using a C-terminal His-tag anchor. Yields of 3-4 mg SRI/l cell culture can be obtained. The absorption and photocycle properties of SRI were similar if not indistinguishable from those of the homologously expressed SRI. A global fit analysis of the photocycle data and the calculation of the spectra of states provided strong evidence for the existence of an N-like intermediate.