Structural highlights
Publication Abstract from PubMed
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 A resolution. The crystal belonged to the triclinic space group P1, with unit-cell parameters a = 77.97, b = 105.28, c = 110.62 A, alpha = 94.6, beta = 109.3, gamma = 108.0 degrees .
Crystallization and preliminary X-ray crystallographic analysis of the inhibitory domain of the tomato mosaic virus resistance protein Tm-1.,Kato M, Kezuka Y, Kobayashi C, Ishibashi K, Nonaka T, Ishikawa M, Katoh E Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Dec;69(Pt 12):1411-4. doi:, 10.1107/S1744309113030819. Epub 2013 Nov 29. PMID:24316842[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kato M, Kezuka Y, Kobayashi C, Ishibashi K, Nonaka T, Ishikawa M, Katoh E. Crystallization and preliminary X-ray crystallographic analysis of the inhibitory domain of the tomato mosaic virus resistance protein Tm-1. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Dec;69(Pt 12):1411-4. doi:, 10.1107/S1744309113030819. Epub 2013 Nov 29. PMID:24316842 doi:http://dx.doi.org/10.1107/S1744309113030819