Purification, crystallization and preliminary crystallographic studies of C-terminal RNA recognition motif (RRM-3) of human ELAV-type RNA-binding protein 3 (ETR-3)

Kashyap Maruthi, Ashwani Sharma, Neel Sarovar Bhavesh

Research output: Contribution to journalArticle


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 (V M) was 6.35 Å3 Da -1, with a solvent content of 80.62%. Initial phases were determined by molecular replacement.

Original languageEnglish (US)
Pages (from-to)1107-1109
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Issue number10
StatePublished - Oct 1 2013
Externally publishedYes



  • C-terminal RNA recognition motif
  • ETR-3
  • human ELAV-type RNA-binding protein 3
  • RRM-3

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

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