System for lyophilization of proteins and metabolites

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We are determining how protein sequence and structure influence protein functions by studying enzymes, antifreeze proteins and osmosensing/osmoregulation systems. Studies of enzymes involved in aromatic hydrocarbon degradation (Seah lab, funded by NSERC) may facilitate the design of biocatalysts to remediate aromatic pollutants or to synthesize enanatiomercially pure pharmaceuticals. It will also facilitate the design of new antimicrobials targeting cholesterol catabolism by the bacteria that cause tuberculosis. Studies of bacterial osmosensing and osmoregulation (Wood lab, funded by NSERC and CIHR) help us to understand how benign and disease-causing Escherichia coli survive exposure to diverse environments while also revealing how human, animal and plant cells survive similar stresses. Studies of cold- and drought-stress proteins (Graether lab, NSERC funded) will help us to understand why some plants are able to tolerate harsh climates while others cannot, with a focus on their complex structure/function relationships. For these studies, we purify proteins, enzymes' substrates and bacterial metabolites that may act to protect cells from osmotic stress. A freeze drier system is requested to concentrate the proteins, substrates and compounds prior to their use in enzyme assays and for structural studies. The system is suitable for samples dissolved in low eutetic solvents, such as acetonitrile or corrosive chemicals, such as acids and ammonia. This system is essential for our research programs and will serve as a unique resource in our Department and University.