Institute of Biochemistry, College of Life Sciences, National Chung Hsing University, Taichung City, Taiwan.
Acta crystallographica. Section D, Biological crystallography 2004 MarType 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 P3(1) (or P3(2)), with unit-cell parameters a = b = 83.5, c = 45.1 A. 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 A resolution with an overall R(merge) of 6.5%.
Tung-Ju Hsieh, Nei-Li Chan. Crystallization and preliminary X-ray crystallographic analysis of the C-terminal domain of ParC protein from Bacillus stearothermophilus. Acta crystallographica. Section D, Biological crystallography. 2004 Mar;60(Pt 3):564-6
PMID: 14993694
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