Cloning, purification, crystallization and preliminary X-ray crystallographic analysis of XC847, a 3'-5' oligoribonuclease from Xanthomonas campestris
| Autor: | Ko-Hsin Chin, Chia-Cheng Chou, Andrew H.-J. Wang, Cheng-Chung Lee, Shan-Ho Chou, Yan-You Wu, Hui-Lin Shr, Fei Philip Gao, Ping-Chiang Lyu |
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| Rok vydání: | 2005 |
| Předmět: |
Amino Acid Motifs
Biophysics Crystallography X-Ray Xanthomonas campestris Biochemistry chemistry.chemical_compound X-Ray Diffraction Structural Biology Genetics Cloning Molecular Gene Pathogen Cloning biology RNA DNA Condensed Matter Physics biology.organism_classification Yeast Crystallography chemistry Crystallization Communications Exoribonucleases Electrophoresis Polyacrylamide Gel Bacteria |
| Zdroj: | Acta crystallographica. Section F, Structural biology and crystallization communications. 61(Pt 10) |
| ISSN: | 1744-3091 |
| Popis: | 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 A. They are tetragonal and belong to space group P4(3)2(1)2, with unit-cell parameters a = b = 67.5, c = 89.8 A. One molecule is present per asymmetric unit. |
| Databáze: | OpenAIRE |
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