In liquid chromatography (LC), discrepancies in liquid properties such as elution strength and viscosity lead to a mismatch between the sample diluent and mobile phase. This mismatch can result in peak deformation, including peak splitting or even breakthrough, particularly when large sample volumes are injected. The formation of a T-junction between sample solution and mobile phase flow stream, a technique previously used in supercritical fluid chromatography, is the key enabler of feed injection in LC.
View Article and Find Full Text PDFProtein production using processed cell lysates is a core technology in synthetic biology and these systems are excellent to produce difficult toxins or membrane proteins. However, the composition of the central lysate of cell-free systems is still a "black box". Escherichia coli lysates are most productive for cell-free expression, yielding several mgs of protein per ml of reaction.
View Article and Find Full Text PDFEscherichia coli C-glycosyltransferase IroB catalyzes the formation of a CC bond between enterobactin and the glucose moiety of UDP-glucose, resulting in the production of mono-, di- and tri-glucosylated enterobactin (MGE, DGE, TGE). To identify catalytic residues, we generated a homology model of IroB from aligned structures of two similar C-glycosyltransferases as templates. Superposition of our homology model onto the structure of a TDP-bound orthologue revealed residue W264 as a possible stabilizer of UDP-glucose.
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