An approach to crystallizing proteins by synthetic symmetrization.

@article{Banatao2006AnAT,
  title={An approach to crystallizing proteins by synthetic symmetrization.},
  author={Diosdado Rey Banatao and Duilio Cascio and Christopher S Crowley and Mark R. Fleissner and Heather L. Tienson and Todd O. Yeates},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2006},
  volume={103 44},
  pages={16230-5}
}
Previous studies of symmetry preferences in protein crystals suggest that symmetric proteins, such as homodimers, might crystallize more readily on average than asymmetric, monomeric proteins. Proteins that are naturally monomeric can be made homodimeric artificially by forming disulfide bonds between individual cysteine residues introduced by mutagenesis. Furthermore, by creating a variety of single-cysteine mutants, a series of distinct synthetic dimers can be generated for a given protein of… CONTINUE READING
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