title: Crystallization and preliminary X-ray diffraction analysis of the barley yellow dwarf virus cap-independent translation element.
abstract: Barley yellow dwarf virus (BYDV) RNA lacks a 5' m(7)GTP cap, yet it is translated efficiently because it contains a 105-base BYDV-like cap-independent translation element (BTE) in the 3' untranslated region (UTR). To understand how the BTE outcompetes the host mRNA for protein-synthesis machinery, its three-dimensional structure is being determined at high resolution. The purification using transcription from DNA containing 2'-O-methyl nucleotides and preliminary crystallographic analyses of the BTE RNA are presented here. After varying the BTE sequence and crystallization-condition optimization, crystals were obtained that diffracted to below 5 Å resolution, with a complete data set being collected to 6.9 Å resolution. This crystal form indexes with an R(merge) of 0.094 in the monoclinic space group C2, with unit-cell parameters a = 316.6, b = 54.2, c = 114.5 Å, α = γ = 90, β = 105.1°.
authors.affiliation: Biochemistry, Biophysics and Molecular Biology Department, Iowa State University, 351 Bessey Hall, Ames, IA 50011, USA.
authors.forename: Jelena J
authors.initials: JJ
authors.lastname: Kraft
authors.forename: Julie A
authors.initials: JA
authors.lastname: Hoy
authors.forename: W Allen
authors.initials: WA
authors.lastname: Miller
mesh_terms: D001483:Base Sequence; D003460:Crystallization; D018360:Crystallography, X-Ray; D017793:Luteovirus / Q000737:chemistry*; D008969:Molecular Sequence Data; D014176:Protein Biosynthesis; D014764:Viral Proteins / Q000737:chemistry*
chemical_list: D014764:Viral Proteins