Abstract
Oligoribonucleases are essential components of RNA and DNA metabolism and close homologues of genes encoding them are found not only in prokaryotes but also in a wide range of eukaryotes, including yeast and humans. Inactivation of the oligoribonuclease gene (orn) can result in cellular lethality. Despite their important biological function, they have been studied little from a structural point of view. In this report, the cloning, expression, crystallization and preliminary X-ray analysis of XC847, a DEDDh-type 3′-5′ oligoribonuclease from the plant pathogen Xanthomonas campestris pv. campestris, a Gram-negative bacterium causing major worldwide disease of cruciferous crops, is described. The XC847 crystals diffracted to a resolution of at least 2.1 Å. They are tetragonal and belong to space group P432 12, with unit-cell parameters a = b = 67.5, c = 89.8 Å. One molecule is present per asymmetric unit. © 2005 International Union of Crystallography All rights reserved.
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CITATION STYLE
Wu, Y. Y., Chin, K. H., Chou, C. C., Lee, C. C., Shr, H. L., Gao, F. P., … Chou, S. H. (2005). Cloning, purification, crystallization and preliminary X-ray crystallographic analysis of XC847, a 3′-5′ oligoribonuclease from Xanthomonas campestris. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 61(10), 902–905. https://doi.org/10.1107/S1744309105027132
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