Finding conditions that optimally stabilize proteins in solution can aid the formation of crystals for X-ray structure determination, since crystallization generally favors 3D lattice assembly from structurally identical objects. Protein molecules are intrinsically dynamic structures that can undergo structural excursions from the ground state as a result of thermal fluctuations. Finding conditions that maximize protein thermal stability has the effect of reducing the structural heterogeneity of protein dynamic states, leading to improved crystal formation.
Chemical screening methods to identify ligands that promote protein stability, protein crystallization, and structure determination. Vedadi M, et. al. Proc Natl Acad Sci USA (2006) 103:15835-15840 [Thermofluor screening of 221 proteins identify to identify ligands that promote stability and aid crystallization.] PMID: 17035505
High resolution crystal structure of the catalytic domain of ADAMTS-5 (aggrecanase-2). Shieh HS, et.al. J Biol Chem (2008) 283:1501-1507 [Thermocycler assay of ADAMTS-5 thermal stability]. PMID: 17991750