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Crystallization of a ZRANB2-RNA complex.

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Dec 01;64(Pt 12):1175-7. Epub 2008 Nov 28
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摘要


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.

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