Crystallization of a ZRANB2-RNA complex

F.E. Loughlin, Mihwa Lee, J.M. Guss, J.P. Mackay

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3 Citations (Scopus)
219 Downloads (Pure)

Abstract

ZRANB2 is a zinc-finger protein that has been shown to influence alternative splice-site selection. The protein comprises a C-terminal arginine/serine-rich domain that interacts with spliceosomal proteins and two N-terminal RanBP2-type zinc fingers that have been implicated in RNA recognition. The second zinc finger bound to a six-nucleotide single-stranded RNA target sequence crystallized in the hexagonal space group P6522 or P6122, with unit-cell parameters a = 54.52, b = 54.52, c = 48.07 Å; the crystal contains one monomeric complex per asymmetric unit. This crystal form has a solvent content of 39% and diffracted to 1.4 Å resolution using synchrotron radiation.
Original languageEnglish
Pages (from-to)1175-1177
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume64
Issue number12
DOIs
Publication statusPublished - 2008

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