Expression, purification and preliminary crystallographic analysis of recombinant human DEAD-box polypeptide 5

Abstract

The DEAD-box RNA helicase DDX5 is involved in many aspects of RNA processing and has been implicated in a number of cellular processes involving alteration of RNA secondary structure. The N-terminal region of DDX5, which contains the conserved domain 1 of the DEAD-box helicases, has been cloned and expressed in Escherichia coli and purified. Here, the crystallization and preliminary diffraction analysis of this region is reported. X-ray diffraction data were processed to a resolution of 2.7 Å. The crystals belonged to space group I222, with unit-cell parameters a = 66.18, b = 73.80, c = 104.00 Å, α = β = γ = 90°. © 2010 International Union of Crystallography All rights reserved.