@article{
 title = {Crystallization of a ZRANB2-RNA complex},
 type = {article},
 year = {2008},
 pages = {1175-1177},
 volume = {64},
 id = {5c489013-8140-39aa-85b6-66fd1e85cec0},
 created = {2023-01-10T01:45:41.371Z},
 file_attached = {false},
 profile_id = {a5a2ab6f-a8b5-3db6-97bc-618752ee4386},
 group_id = {bc1ab1d4-9e57-37e6-9fb5-435fca0ee9d2},
 last_modified = {2023-01-10T01:45:41.371Z},
 read = {false},
 starred = {false},
 authored = {false},
 confirmed = {false},
 hidden = {false},
 private_publication = {false},
 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. © International Union of Crystallography 2008.},
 bibtype = {article},
 author = {Loughlin, F.E. and Lee, M. and Guss, J.M. and Mackay, J.P.},
 doi = {10.1107/S1744309108036993},
 journal = {Acta Crystallographica Section F: Structural Biology and Crystallization Communications},
 number = {12}
}

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