Crystallization and preliminary X-ray crystallographic analysis of the C-terminal domain of ParC protein from Bacillus stearothermophilus

Authors: Hsieh, Tung-Ju; Chan, Nei-Li

Source: Acta Crystallographica Section D, Volume 60, Number 3, March 2004 , pp. 564-566(3)

Publisher: Blackwell Publishing

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Abstract:

Type IIA topoisomerases are multidomain enzymes composed of four major domains: the ATPase domain, the TOPRIM domain, the DNA-cleavage/religation domain and the C-terminal domain (CTD). Although crystal structures of the first three domains are available, the three-dimensional structure of the less-conserved CTD has yet to be determined. In order to provide a three-dimensional structure of this structurally uncharacterized region, the 36 kDa CTD of ParC protein, the DNA-cleavage/religation subunit of topoisomerase IV, from Bacillus stearothermophilus has been cloned, purified and crystallized. The crystals belonged to the trigonal space group P3₁ (or P3₂), with unit-cell parameters a = b = 83.5, c = 45.1 Å. The asymmetric unit contains one molecule and the solvent content is 51.2%. A 98.9% complete native data set has been collected from a frozen crystal to 2.0 Å resolution with an overall R_merge of 6.5%.

Keywords: ParC-CTD; DNA topoisomerase IV; type IIA topoisomerase

Document Type: Research article

DOI: 10.1107/S0907444903029779

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