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Acta Crystallogr F Struct Biol Commun. 2014 Dec 1;70(Pt 12):1688-92. doi: 10.1107/S2053230X14024935. Epub 2014 Nov 28.

Expression, purification and crystallization of two endonuclease III enzymes from Deinococcus radiodurans.

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Chemistry Department, NorStruct, UiT The Arctic University of Norway, Forskningsparken 3, 9037 Tromsø, Norway.
Structural Biology Group, European Synchrotron Radiation Facility, 71 Avenue des Martyrs, 38043 Grenoble, France.


Endonuclease III is a bifunctional DNA glycosylase that removes a wide range of oxidized bases in DNA. Deinococcus radiodurans is an extreme radiation-resistant and desiccation-resistant bacterium and possesses three genes encoding endonuclease III enzymes in its genome: DR2438 (EndoIII-1), DR0289 (EndoIII-2) and DR0982 (EndoIII-3). Here, EndoIII-1 and an N-terminally truncated form of EndoIII-3 (EndoIII-3Δ76) have been expressed, purified and crystallized, and preliminary X-ray crystallographic analyses have been performed to 2.15 and 1.31 Å resolution, respectively. The EndoIII-1 crystals belonged to the monoclinic space group C2, with unit-cell parameters a = 181.38, b = 38.56, c = 37.09 Å, β = 89.34° and one molecule per asymmetric unit. The EndoIII-3Δ76 crystals also belonged to the monoclinic space group C2, but with unit-cell parameters a = 91.47, b = 40.53, c = 72.47 Å, β = 102.53° and one molecule per asymmetric unit. The EndoIII-1 structure was determined by molecular replacement, while the truncated EndoIII-3Δ76 structure was determined by single-wavelength anomalous dispersion phasing. Refinement of the structures is in progress.


Deinococcus radiodurans; EndoIII-1; EndoIII-3; endonuclease III

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