To demonstrate the utility of DXMS analysis for crystallographic construct optimization, the exchange patterns of 21 different Thermotoga maritima proteins were measured in collaboration with the Joint Center for Structural Genomics (JCSG) . Among the 21 proteins studied, 12 crystallized readily and the remaining nine crystallized poorly. While most of the crystallizable proteins contained no substantial disordered regions, four of the nine poorly crystallizing proteins contained 10% or more of their sequence in disordered regions. The exchange pattern of TM0160 is an example of disorder within a poorly crystallizing protein (Fig. 12.3a). The largest disordered region of this protein was seen to be at its C-terminus, suggesting a straightforward route to construct optimization by deletion of the disordered C-terminus.
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