Open AccessCloning, purification, crystallization and preliminary X‐ray crystallographic analysis of the N‐terminal domain of DEAD‐box RNA helicase from Staphylococcus aureus strain Mu50
Author(s) -
Lee Soo Young,
Jung Ha Yun,
Kim TaeO,
Im DongWon,
You KiYoung,
Back JangMi,
Kim Yangmee,
Kim Hak Jun,
Shin Whanchul,
Heo YongSeok
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110043149
Subject(s) - rna , helicase , deinococcus radiodurans , rna helicase a , ribosome , strain (injury) , undulator , escherichia coli , rna splicing , chemistry , crystallography , biology , dna , microbiology and biotechnology , physics , biochemistry , optics , gene , radiation , anatomy
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 P 1, 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 Å 3 Da −1 and a solvent content of 56.1%.