Crystallization of E. coli RuvA gives insights into the symmetry of a Holliday junction/protein complex.
The E. coli protein RuvA (resistance to ultraviolet light) has been overexpressed in E. coli, purified and crystallized using the hanging-drop vapour-diffusion method with sodium chloride as the precipitant. The crystals, which diffract to beyond 1.9 A, belong to the tetragonal system, space group P4 with unit-cell dimensions of a = 83.7, c = 33.1 A with a monomer in the asymmetric unit. RuvA is known to be a tetramer and thus the crystal symmetry implies that its quaternary structure will be based on fourfold rotation symmetry rather than 222 symmetry. This is consistent with electron microscopy data on Holliday junction DNA complexes and implies that the arms of the four DNA duplexes involved in recombination adopt fourfold rotation symmetry.
Krebs Institute for Biomolecular Research, Department of Molecular Biology and Biotechnology, The University of Sheffield, England.
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Sedelnikova
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