Crystallization of the N-terminal ankyrin repeat domain of the 2-5A-dependent endoribonuclease, RNase L.
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 2-5 Angstroms. The crystals belong to an orthorhombic space group P2(1)2(1)2(1) with cell dimensions of a = 63.11 Angstroms, b = 73.03 Angstroms, and c = 82.64 Angstroms. There is one molecule per asymmetric unit. The crystals diffract to at least 2.1 Angstroms resolution using synchrotron radiation and are suitable for X-ray structure analysis at high resolution.
Tanaka
Nobutada
N
School of Pharmaceutical Sciences, Showa University, Tokyo, Japan. ntanaka@pharm.showa-u.ac.jp
Nakanishi
Masayuki
M
Kusakabe
Yoshio
Y
Goto
Yoshikuni
Y
Kitade
Yukio
Y
Nakamura
Kazuo T
KT
D017089:Ankyrin Repeat; D003460:Crystallization; D018360:Crystallography, X-Ray; D004722:Endoribonucleases / Q000737:chemistry*; D006801:Humans
D004722:Endoribonucleases; C031956:2-5A-dependent ribonuclease