title: Crystallization of the N-terminal ankyrin repeat domain of the 2-5A-dependent endoribonuclease, RNase 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 2-5 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.
authors.affiliation: School of Pharmaceutical Sciences, Showa University, Tokyo, Japan. ntanaka@pharm.showa-u.ac.jp
authors.forename: Nobutada
authors.initials: N
authors.lastname: Tanaka
authors.forename: Masayuki
authors.initials: M
authors.lastname: Nakanishi
authors.forename: Yoshio
authors.initials: Y
authors.lastname: Kusakabe
authors.forename: Yoshikuni
authors.initials: Y
authors.lastname: Goto
authors.forename: Yukio
authors.initials: Y
authors.lastname: Kitade
authors.forename: Kazuo T
authors.initials: KT
authors.lastname: Nakamura
mesh_terms: D017089:Ankyrin Repeat; D003460:Crystallization; D018360:Crystallography, X-Ray; D004722:Endoribonucleases / Q000737:chemistry*; D006801:Humans
chemical_list: D004722:Endoribonucleases; C031956:2-5A-dependent ribonuclease