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Purification, crystallization and preliminary X‐ray diffraction analysis of DNA damage response A protein from Deinococcus radiodurans

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DNA damage response A protein (DdrA) from Deinococcus radiodurans has been suggested to be involved in DNA‐repair processes through binding to 3′‐ends of single‐stranded DNA, thereby protecting the ends from nuclease digestion. In this study, a recombinant C‐terminally truncated form of D. radiodurans DdrA (DdrA157) comprising the first 157 residues of DdrA was expressed in Escherichia coli, purified and crystallized. Single crystals of DdrA157 were obtained by the hanging‐drop method at 293 K. The crystal belonged to the monoclinic space group P21, with unit‐cell parameters a = 46.31, b = 180.26, c = 114.17 Å, β = 90.02°. The crystal was expected to contain 14 molecules in the asymmetric unit. Diffraction data were collected to 2.35 Å resolution on beamline BL‐5 at Photon Factory and initial phase determinations were attempted by the molecular‐replacement method using the human Rad52 structure.
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Keywords: DNA damage response A; DNA repair; Deinococcus radiodurans

Document Type: Research Article

Affiliations: Gene Resource Research Group, Life Science and Biotechnology Division, Quantum Beam Science Directorate, Japan Atomic Energy Agency, 1233 Watanuki, Takasaki, Gunma 370-1292, Japan

Publication date: December 1, 2010

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