Abstract
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: ankyrin repeat, a system, interferon, ribonuclease l
Protein & Peptide Letters
Title: Crystallization of the N-Terminal Ankyrin Repeat Domain of the 2-5ADependent Endoribonuclease, RNase L
Volume: 12 Issue: 4
Author(s): Nobutada Tanaka, Masayuki Nakanishi, Yoshio Kusakabe, Yoshikuni Goto, Yukio Kitade and Kazuo T. Nakamura
Affiliation:
Keywords: ankyrin repeat, a system, interferon, ribonuclease l
Abstract: 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.
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Cite this article as:
Tanaka Nobutada, Nakanishi Masayuki, Kusakabe Yoshio, Goto Yoshikuni, Kitade Yukio and Nakamura T. Kazuo, Crystallization of the N-Terminal Ankyrin Repeat Domain of the 2-5ADependent Endoribonuclease, RNase L, Protein & Peptide Letters 2005; 12 (4) . https://dx.doi.org/10.2174/0929866053765734
DOI https://dx.doi.org/10.2174/0929866053765734 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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