Crystallization of a ZRANB2-RNA complex

Fionna E. Loughlin, Mihwa Lee, J. Mitchell Guss, Joel P. Mackay

Research output: Contribution to journalArticleResearchpeer-review

2 Citations (Scopus)


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
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Issue number12
Publication statusPublished - 28 Nov 2008
Externally publishedYes


  • RanBP2-type zinc fingers
  • RNA-binding proteins
  • Splicing factors

Cite this