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

ABSTRACT: 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, ?=69.54, ?=66.54, ?=87.32°. The unit cell contained six molecules, with a corresponding VM of 2.91?Å3?Da(-1) and a solvent content of 56.1%.

SUBMITTER: Lee SY 

PROVIDER: S-EPMC2998381 | biostudies-literature | 2010 Dec

REPOSITORIES: biostudies-literature