Crystallization and preliminary X-ray analysis of the helicase domains of Vasa complexed with RNA and an ATP analogue

Acta Crystallogr D Biol Crystallogr. 2004 Feb;60(Pt 2):320-2. doi: 10.1107/S0907444903025897. Epub 2004 Jan 23.

Abstract

The helicase fragment of Vasa was purified and its RNA-binding activity was examined by a UV cross-linking assay. The fragment was crystallized in complex with poly(U) RNA (U(10)) and a non-hydrolyzable analogue of ATP. The crystal belonged to space group P2(1), with unit-cell parameters a = 71.06, b = 142.35, c = 130.47 A, beta = 90.86 degrees. The cryocooled crystal diffracted to about 2.2 A using synchrotron radiation from station BL41XU at SPring-8.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphate / chemistry*
  • Animals
  • Cross-Linking Reagents / pharmacology
  • Crystallography, X-Ray
  • DEAD-box RNA Helicases
  • Drosophila Proteins
  • Drosophila melanogaster / metabolism
  • Humans
  • Poly U
  • Protein Binding
  • Protein Structure, Tertiary
  • RNA / chemistry*
  • RNA Helicases / chemistry*
  • RNA, Messenger / metabolism
  • Ultraviolet Rays

Substances

  • Cross-Linking Reagents
  • Drosophila Proteins
  • RNA, Messenger
  • Poly U
  • RNA
  • Adenosine Triphosphate
  • DDX4 protein, human
  • vas protein, Drosophila
  • DEAD-box RNA Helicases
  • RNA Helicases