Publication Type:Journal Article
Source:Acta Crystallogr Sect F Struct Biol Cryst Commun, Volume 67, Number Pt 5, p.561-4 (2011)
ISBN:1744-3091 (Electronic)<br/>1744-3091 (Linking)
Keywords:Base Sequence, Crystallization, Crystallography, X-Ray, Luteovirus/ chemistry, Molecular Sequence Data, Protein Biosynthesis, Viral Proteins/ chemistry
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 A resolution, with a complete data set being collected to 6.9 A 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 A, alpha = gamma = 90, beta = 105.1 degrees .
Kraft, Jelena J<br/>Hoy, Julie A<br/>Miller, W Allen<br/>R01 GM067104/GM/NIGMS NIH HHS/United States<br/>R01 GM067104-06S1/GM/NIGMS NIH HHS/United States<br/>Research Support, American Recovery and Reinvestment Act<br/>Research Support, N.I.H., Extramural<br/>England<br/>Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 May 1;67(Pt 5):561-4. doi: 10.1107/S1744309111007196. Epub 2011 Apr 21.