LEX - a true high throughput bioreactor system

Laboratory scale cell cultures are often grown in shakers, which have limits in rates and controllability of oxygenation, mixing and temperature control. Moreover, shakers are large, heavy instruments which do not facilitate monitoring of growth. On the other hand, traditional bioreactors which provide more direct monitoring and control of cell cultures are typically an order of magnitude or higher in costs and therefore typically impractical for high throughput experimentation.

Harbinger's LEX system replaces traditional medium-low throughput mechanical shakers with an ultra high-throughput bench-top bioreactor system. It was developed at the Structural Genomics Consortium and used by the SGC to express over a thousand of novel recombinant proteins, including hundreds of Plasmodium proteins previously considered to be mostly unsuitable for expression in E. coli [1,2].

Key features:

• Capacity to run 24 individual 2L bottle experiments in parallel in a single LEX system.
• 4 times the capacity of a traditional shaker at the same cost and smaller footprint.
• 1 m x .75 m (3.5 foot x 2.5 foot) bench-top footprint for efficient use of lab space.
• Tight reaction kinetics control and temperature shock capabilities through very efficient water-bath temperature control and ice quenching.
• Individualized control of mixing and oxygenation for each bottle allowing optimized culture aeration.
• Real-time bioreactor control with in-situ optical density monitoring (available as an upgrade).
• Ease of use with quick-disconnects (for rapid setup) and fully sterilizable components.
• Multi-stage, replaceable carbon+HEPA filter forced-air hood with enclosure eliminating unpleasant odours and harmful airborne by-products.
• Optimized for high-yield cell-culture growth and recombinant protein expression.

Contact us to find our more about our LEX bioreactor system.

References

1. Vedadi M et al. Genome-scale protein expression and structural biology of Plasmodium falciparum and related Apicomplexan organisms. Mol Biochem Parasitol. 2007 Jan;151(1):100-10.
2. Dufe et al. Crystal structure of Plasmodium falciparum spermidine synthase in complex with the substrate decarboxylated S-adenosylmethionine and the potent inhibitors 4MCHA and AdoDATO. J Mol Biol. 2007 Oct 12;373(1):167-77.
3. Graslund et al. The use of systematic N- and C-terminal deletions to promote production and structural studies of recombinant proteins. Protein Expr Purif. 2007 Nov 22.