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Protein Crystals
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.
Thermofluor-based high-throughput stability optimization of proteins for structural studies. Ericsson UB, et.al. Anal Biochem (2006) 357:289-298 [Thermoflour for optimization of crystallization conditions] PMID: 16962548 [PDF]
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
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