2hum
From Proteopedia
Crystal structure of T4 Lysozyme D72C synthetic dimer
Overview
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.
About this Structure
2HUM is a Single protein structure of sequence from Enterobacteria phage t4. Full crystallographic information is available from OCA.
Reference
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. 2006 Oct 31;103(44):16230-5. Epub 2006 Oct 18. PMID:17050682 Page seeded by OCA on Wed May 14 11:38:18 2008
