Publication date: 8th October 2020
Until now, the research on the structure and function of cyanobacterial PSI monomers was hampered by the lack of a suitable purification method for the monomeric complex. While previous purification methods included harsh treatment of the protein such as exposure to high temperatures to achieve monomerization, they could yield only a minor protein amount, mostly accompanied by a partial loss of protein subunits and activity [1],[3]. We hereby propose a protocol for the efficient purification of “native-like” PSI monomers from the thermophilic cyanobacterium Thermosynechococcus elongatus at gentle conditions, with a monomerization efficiency of approximately 95%. Thereby, monomerization is achieved by the extraction with 0.5% LDAO after a prior incubation at 2 M AMS, yielding over ten times more protein than recent protocols for the isolation of PSI monomers [2]. High purity and sample quality could be proven via activity measurements, mass spectrometry analysis and negative stain transmission electron microscopy, providing a sample quality suitable for protein crystallization.
This research was funded by the German Research Council (DFG) in the framework of the Research Training Group of Microbial Substrate Conversion (‘MiCon’, GRK 2341).
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