Synthetic symmetrization in the crystallization and structure determination of CelA from Thermotoga maritima.

ABSTRACT: Protein crystallization continues to be a major bottleneck in X-ray crystallography. Previous studies suggest that symmetric proteins, such as homodimers, might crystallize more readily than monomeric proteins or asymmetric complexes. Proteins that are naturally monomeric can be made homodimeric artificially. Our approach is to create homodimeric proteins by introducing single cysteines into the protein of interest, which are then oxidized to form a disulfide bond between the two monomers. By introducing the single cysteine at different sequence positions, one can produce a variety of synthetically dimerized versions of a protein, with each construct expected to exhibit its own crystallization behavior. In earlier work, we demonstrated the potential utility of the approach using T4 lysozym

SUBMITTER: Forse GJ 

PROVIDER: S-EPMC3047073 | biostudies-literature | 2011 Jan

REPOSITORIES: biostudies-literature