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. 2009 Jun 1;106(24):9556–9563. doi: 10.1073/pnas.0904877106

Fig. 6.

Fig. 6.

HSP90.2rsp mutant proteins retain dimerization capability. Chemical cross-linking of wild-type and mutant forms of HSP90.2 in the presence of ADP or the nonhydrolysable ATP analog AMP-PNP. All variants of HSP90.2 are unable to dimerize in the presence of ADP. However, although no lra mutant variants (A) are able to dimerize even in the presence of AMP-PNP, both rsp mutant variants (B) can dimerize in the presence of AMP-PNP. The experiment was performed with an HSP90 concentration of 0.25 mg/mL, 15 molar equivalents of DMS, and 10 mM nucleotide.