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Crystallization of the N-Terminal Ankyrin Repeat Domain of the 2-5ADependent Endoribonuclease, RNase L

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The N-terminal ankyrin repeat domain of the 2'-5'-linked oligoadenylate (2-5A)-dependent endoribonuclease, RNase L, has been crystallized by the hanging-drop vapor diffusion method in the presence of 2-5A. The crystals belong to an orthorhombic space group P212121 with cell dimensions of a = 63.11 Å, b = 73.03 Å, and c = 82.64 Å. There is one molecule per asymmetric unit. The crystals diffract to at least 2.1 Åresolution using synchrotron radiation and are suitable for X-ray structure analysis at high resolution.

Keywords: a system; ankyrin repeat; interferon; ribonuclease l

Document Type: Review Article


Affiliations: School of Pharmaceutical Sciences, Showa University, Tokyo 142-8555, Japan.

Publication date: May 1, 2005

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.

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