Acta Crystallographica Section F

Structural Biology and Crystallization Communications

Volume 61, Part 10 (October 2005)

crystallization communications

Acta Cryst. (2005). F61, 902-905 [ doi:10.1107/S1744309105027132 ]

Cloning, purification, crystallization and preliminary X-ray crystallographic analysis of XC847, a 3'-5' oligoribonuclease from Xanthomonas campestris

Y.-Y. Wu, K.-H. Chin, C.-C. Chou, C.-C. Lee, H.-L. Shr, F. P. Gao, P.-C. Lyu, A. H.-J. Wang and S.-H. Chou

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 P4₃2₁2, with unit-cell parameters a = b = 67.5, c = 89.8 Å. One molecule is present per asymmetric unit.

Keywords: 3'-5' oligoribonucleases; Orn; DEDDh; Xanthomonas campestris.