pTWIN-MBP1 has the E. coli maltose binding protein (MBP) (2) fused between the modified Ssp DnaB (3) and Mxe GyrA inteins (4). The presence of the chitin binding domain from Bacillus circulans (5,6) facilitates purification. The pTWIN-MBP1 vector permits the isolation of a circular MBP species (1). The double-stranded vector is 8,518 base pairs in length.
pTWIN-MBP1 contains two mini-inteins, one derived from the Synechocystis sp DnaB intein (154 amino acids) (7) and the other from the Mycobacterium xenopi GyrA intein (198 amino acids) (8).
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