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Cloning, purification, crystallization and preliminary X-ray crystallographic analysis of XC847, a 3′-5′ oligoribonuclease from Xanthomonas campestris
Journal article   Open access   Peer reviewed

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

Yan-You Wu, Ko-Hsin Chin, Chia-Cheng Chou, Cheng-Chung Lee, Hui-Lin Shr, Fei Philip Gao, Ping-Chiang Lyu, Andrew H.-J. Wang and Shan-Ho Chou
Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol.61(10), pp.902-905
2005

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 P4 3 2 1 2, 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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https://doi.org/10.1107/S1744309105027132View
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