Crystallization of the N-terminal ankyrin repeat domain of the 2-5A-dependent endoribonuclease, RNase L

被引：6

作者：

Tanaka, N ^{[1
]}

Nakanishi, M

Kusakabe, Y

Goto, Y

Kitade, Y

Nakamura, KT

机构：

[1] Showa Univ, Sch Pharmaceut Sci, Tokyo 1428555, Japan

[2] Gifu Univ, Fac Engn, Dept Biomol Sci, Gifu 5011193, Japan

来源：

PROTEIN AND PEPTIDE LETTERS | 2005年 / 12卷 / 04期

关键词：

ankyrin repeat; 2-5A system; interferon; ribonuclease L;

D O I：

10.2174/0929866053765734

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The N-terminal ankyrin repeat domain of the 2'-5'-linked oligoadenylate (2-5A)-dependent endoribonuclcase. 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 P2(1)2(1)2(1) with cell dimensions of a = 63.11 &ANGS;, b = 73.03 &ANGS;, and c = 82.64 &ANGS;. There is one molecule per asymmetric unit. The crystals diffract to at least 2.1 &ANGS; resolution using synchrotron radiation and are suitable for X-ray structure analysis at high resolution.

引用

页码：387 / 389

页数：3

共 13 条

[1]

[Anonymous], ACTA CRYSTALLOGR D

[2] A bipartite model of 2-5A-dependent RNase L [J].