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Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Dec;69(Pt 12):1411-4. doi: 10.1107/S1744309113030819. Epub 2013 Nov 29.

Crystallization and preliminary X-ray crystallographic analysis of the inhibitory domain of the tomato mosaic virus resistance protein Tm-1.

Author information

  • 1Biomolecular Research Unit, National Institute of Agrobiological Sciences, Tsukuba, Ibaraki 305-0856, Japan.

Abstract

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 P1, with unit-cell parameters a = 77.97, b = 105.28, c = 110.62 Å, α = 94.6, β = 109.3, γ = 108.0°.

KEYWORDS:

Tm-1; Tomato mosaic virus; replication protein

PMID:
24316842
PMCID:
PMC3855732
DOI:
10.1107/S1744309113030819
[PubMed - indexed for MEDLINE]
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