Cloning, purification, crystallization and preliminary X-ray crystallographic analysis of XC847, a 3′-5′ oligoribonuclease from Xanthomonas campestris
Acta Crystallographica Section F
Volume 61, Issue 10, pages 902–905, October 2005
How to Cite
Wu, Y.-Y., Chin, K.-H., Chou, C.-C., Lee, C.-C., Shr, H.-L., Gao, F. P., Lyu, P.-C., Wang, A. H.-J. and 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, 61: 902–905. doi: 10.1107/S1744309105027132
- 3′-5′ oligoribonucleases;
- Xanthomonas campestris.
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 P43212, with unit-cell parameters a = b = 67.5, c = 89.8 Å. One molecule is present per asymmetric unit.