Expression and purification of recombinant proteins are important for the structure–function study of phytochromes. However, it is difficult to purify phytochrome proteins from natural sources or using a bacterial expression system, due to the presence of multiple phytochrome species and low expression and solubility, respectively. Here we describe the expression of recombinant full-length plant phytochromes in the yeast Pichia pastoris, and the spectral analysis of chromophore-assembled phytochromes before and after the purification by streptavidin affinity chromatography.
CITATION STYLE
Han, Y. J., Cho, J. Y., & Kim, J. I. (2019). Expression, Purification, and Spectral Characterization of Phytochromes. In Methods in Molecular Biology (Vol. 2026, pp. 95–111). Humana Press Inc. https://doi.org/10.1007/978-1-4939-9612-4_7
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