pET28a-HsLARP6

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	Expression constructs for the two fish LARP6 proteins were transformed into chemically-competent BL21(DE3) or Rosetta(DE3) expression lines of Escherichia coli (the former a kind gift of R. McLean, Texas State University). One liter cultures were grown at 37 °C until an optical density of 0.6 – 0.8, then cooled on ice before inducing expression with 1 mM IPTG for 8 hours at 18°C.	Cells were harvested by centrifugation at 5000×g at 4°C for 5 min. The cell pellet was transferred to a conical vial and stored at -20°C until purification.

Protocol tips
Expression constructs for the two fish LARP6 proteins were transformed into chemically-competent BL21(DE3) or Rosetta(DE3) expression lines of Escherichia coli (the former a kind gift of R. McLean, Texas State University). One liter cultures were grown at 37 °C until an optical density of 0.6 – 0.8, then cooled on ice before inducing expression with 1 mM IPTG for 8 hours at 18°C.
Downstream tips
Cells were harvested by centrifugation at 5000×g at 4°C for 5 min. The cell pellet was transferred to a conical vial and stored at -20°C until purification.

Publication protocol

The expression of human LARP6 was performed as described [15]. Expression constructs for the two fish LARP6 proteins were transformed into chemically-competent BL21(DE3) or Rosetta(DE3) expression lines of Escherichia coli (the former a kind gift of R. McLean, Texas State University). One liter cultures were grown at 37 °C until an optical density of 0.6 – 0.8, then cooled on ice before inducing expression with 1 mM IPTG for 8 hours at 18°C. Cells were harvested by centrifugation at 5000×g at 4°C for 5 min. The cell pellet was transferred to a conical vial and stored at -20°C until purification.

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