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An approach to crystallizing proteins by synthetic symmetrization.

Banatao DR, Cascio D, Crowley CS, Fleissner MR, Tienson HL, Yeates TO
Proc Natl Acad Sci U S A 103 16230-5 (2006)
Related entries: 2hul, 2hum

Cited: 48 times
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Abstract

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 interest, with each expected to gain advantage from its added symmetry and to exhibit a crystallization behavior distinct from the other constructs. This strategy was tested on phage T4 lysozyme, a protein whose crystallization as a monomer has been studied exhaustively. Experiments on three single-cysteine mutants, each prepared in dimeric form, yielded numerous novel crystal forms that cannot be realized by monomeric lysozyme. Six new crystal forms have been characterized. The results suggest that synthetic symmetrization may be a useful approach for enlarging the search space for crystallizing proteins.

Articles - 2huk mentioned but not cited (2)

  1. An approach to crystallizing proteins by synthetic symmetrization. Banatao DR, Cascio D, Crowley CS, Fleissner MR, Tienson HL, Yeates TO. Proc Natl Acad Sci U S A 103 16230-16235 (2006)
  2. Homodimeric Protein-Polymer Conjugates via the Tetrazine-trans-Cyclooctene Ligation. Lorenzo MM, Decker CG, Kahveci MU, Paluck SJ, Maynard HD. Macromolecules 49 30-37 (2016)


Reviews citing this publication (8)

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