Purification, crystallization and preliminary X-ray analysis of the catalytic domain of the Escherichia coli tRNase colicin D
- Department of Biotechnology, The University of Tokyo, Yayoi 1-1-1, Bunkyo-ku, Tokyo 113-8657 (Japan)
- Department of Bioscience, Tokyo University of Agriculture, Setagaya-ku, Tokyo 156-8502 (Japan)
The tRNase domain of colicin D, which is specific to tRNA{sup Arg}s, has been crystallized. A diffraction data set has been collected to a resolution of 1.05 Å. The tRNase domain of colicin D, which cleaves only tRNA{sup Arg}s at the 3′ side of their anticodon loops, has been expressed in Escherichia coli with its inhibitor protein and purified to a form free from the inhibitor using a low-pH buffer. Crystals were obtained by the hanging-drop vapour-diffusion method at 278 K from a buffer containing 100 mM Tris–HCl pH 8.5, 22% PEG MME 2000 and 1 mM nickel(II) chloride. Diffraction data to 1.05 Å resolution were collected at BL41XU, SPring-8. The crystals belong to space group P2{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 34.7, b = 65.5, c = 96.5 Å.
- OSTI ID:
- 22356246
- Journal Information:
- Acta Crystallographica. Section F, Vol. 62, Issue Pt 1; Other Information: PMCID: PMC2150931; PMID: 16511255; PUBLISHER-ID: ll5039; OAI: oai:pubmedcentral.nih.gov:2150931; Copyright (c) International Union of Crystallography 2006; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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