Open AccessCrystallization and preliminary X‐ray crystallographic analysis of the inhibitory domain of the tomato mosaic virus resistance protein Tm‐1
Author(s) -
Kato Masahiko,
Kezuka Yuichiro,
Kobayashi Chihoko,
Ishibashi Kazuhiro,
aka Takamasa,
Ishikawa Masayuki,
Katoh Estuko
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113030819
Subject(s) - triclinic crystal system , crystallization , crystallography , x ray , c terminus , domain (mathematical analysis) , tobacco mosaic virus , crystal (programming language) , crystal structure , resolution (logic) , x ray crystallography , chemistry , diffraction , virus , biology , virology , physics , biochemistry , amino acid , optics , mathematics , artificial intelligence , mathematical analysis , programming language , organic chemistry , computer science
Tm‐1, an inhibitor protein of Tomato mosaic virus RNA replication, contains two conserved domains: an uncharacterized domain at its N‐terminus and a TIM‐barrel‐like domain at its C‐terminus. The N‐terminal domain of Tm‐1 has an inhibitory activity and its three‐dimensional structure has not been determined. Here, the crystallization and preliminary X‐ray diffraction of the N‐terminal domain of Tm‐1 are reported. A three‐wavelength MAD data set was collected from a selenomethionine‐labelled crystal and processed to 2.7 Å resolution. The crystal belonged to the triclinic space group P 1, with unit‐cell parameters a = 77.97, b = 105.28, c = 110.62 Å, α = 94.6, β = 109.3, γ = 108.0°.