Cloning, purification, crystallization and preliminary X-ray crystallographic analysis of the N-­terminal domain of DEAD-box RNA helicase from Staphylococcus aureus strain Mu50

DEAD-box helicases are enzymes with an ATP-dependent RNA-unwinding function that are involved in a variety of cellular processes including RNA splicing, ribosome biogenesis and RNA degradation. In this study, the N-­terminal domain of DEAD-box RNA helicase from Staphylococcus aureus strain Mu50 was overexpressed in Escherichia coli, purified and crystallized. Diffraction data were collected to 2.60 Å resolution using a synchrotron-radiation source. The crystal belonged to space group P1, with unit-cell parameters a = 70.81, b = 80.23, c = 86.25 Å, α = 69.54, β = 66.54, γ = 87.32°. The unit cell contained six molecules, with a corresponding V_M of 2.91 ų Da⁻¹ and a solvent content of 56.1%.