Crystallization of a ZRANB2-RNA complex.
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 P6(5)22 or P6(1)22, with unit-cell parameters a = 54.52, b = 54.52, c = 48.07 A; the crystal contains one monomeric complex per asymmetric unit. This crystal form has a solvent content of 39% and diffracted to 1.4 A resolution using synchrotron radiation.
Loughlin
Fionna E
FE
School of Molecular and Microbial Biosciences, University of Sydney, Sydney, NSW, Australia.
Lee
Mihwa
M
Guss
J Mitchell
JM
Mackay
Joel P
JP
D001665:Binding Sites; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans; D012313:RNA / Q000737:chemistry* / Q000378:metabolism; D016601:RNA-Binding Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
D016601:RNA-Binding Proteins; C486373:ZRANB2 protein, human; D012313:RNA