Open AccessCrystallization of a ZRANB2–RNA complex
Author(s) -
Loughlin Fionna E.,
Lee Mihwa,
Guss J. Mitchell,
Mackay Joel P.
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108036993
Subject(s) - crystallography , crystallization , zinc finger , rna , monomer , zinc , chemistry , sequence (biology) , crystal structure , biochemistry , gene , polymer , organic chemistry , transcription factor
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 P 6 5 22 or P 6 1 22, 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.