ArticleActa crystallographica. Section F, Structural biology and crystallization communications2013
Purification, crystallization and preliminary crystallographic studies of C-terminal RNA recognition motif (RRM-3) of human ELAV-type RNA-binding protein 3 (ETR-3).
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Human embryonically lethal abnormal vision (ELAV)-type RNA-binding protein 3 (ETR-3) has been implicated in many aspects of RNA-processing events including alternative splicing, stability, editing and translation. RNA recognition motif 3 (RRM-3) is an independent C-terminal RNA-binding domain of ETR-3 that preferentially binds to UG-rich repeats of the nuclear or cytoplasmic pre-mRNA, and along with the other domains mediates the inclusion of cardiac troponin T (c-TNT) exon 5 in embryonic muscle, which is otherwise excluded in the adult. In the present study, RRM-3 was cloned, overexpressed, purified and crystallized by the hanging-drop vapour-diffusion method. The crystals diffracted to 3 Å resolution at the home source and belonged to space group P2₁3, with unit-cell parameters a=b=c=118.5 Å, α=β=γ=90°. There were two molecules of RRM-3 in the asymmetric unit and the calculated Matthews coefficient (VM) was 6.35 Å3 Da(-1), with a solvent content of 80.62%. Initial phases were determined by molecular replacement.
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