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. 2009 Dec 20;3(1):84–92. doi: 10.1111/j.1751-7915.2009.00150.x

Figure 2.

Figure 2

Size exclusion chromatography of purified recombinant AxeA, revealing active homodimeric and homohexameric forms of the enzyme. The elution volumes of the two symmetric peaks correspond to native molecular masses of 74.5 and 229.1 kDa respectively (for details see Experimental procedures). Insert: Oligomeric state of AxeA as derived from crystallographic data (PDB ID: 1vlq) which suggests 12 monomers arranged as two homohexamers in the asymmetric unit of the protein crystal.