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. 2007 Aug;16(8):1617–1627. doi: 10.1110/ps.062749007

Figure 4.

Figure 4.

SDS-PAGE of cross-linked wild-type InhA and the interface B lysine mutants. (A) SDS-PAGE of wild-type InhA and three lysine mutants, Lys118Arg, Lys132Arg, and Lys165Arg, after cross-linking with BS3. The three lysines are thought to form cross-links over interface B. The wild-type InhA and all single mutants appear identical, giving monomers (30.7 kDa) in the absence of cross-linker (−), and monomers, dimers (61.3 kDa), and tetramers (122.7 kDa) in the presence of cross-linker (+). (B) Cross-linking of the Lys118Arg/Lys132Arg, Lys118Arg/Lys165Arg, and Lys132Arg/Lys165Arg double mutants. No tetramer can be observed for the Lys118Arg/Lys165Arg double mutant.