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 VM of 2.91 Å3 Da(-1) and a solvent content of 56.1%.
Department of Chemistry, Konkuk University, Hwayang-dong, Gwangjin-gu, Seoul 143-701, Republic of Korea.
Soo Young
SY
Lee
Ha Yun
HY
Jung
Tae-O
TO
Kim
Dong-Won
DW
Im
Ki-Young
KY
You
Jang-Mi
JM
Back
Yangmee
Y
Kim
Hak Jun
HJ
Kim
Whanchul
W
Shin
Yong-Seok
YS
Heo
D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification*; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D053487:DEAD-box RNA Helicases / Q000737:chemistry* / Q000302:isolation & purification*; D017434:Protein Structure, Tertiary; D013211:Staphylococcus aureus / Q000201:enzymology*
D001426:Bacterial Proteins; D053487:DEAD-box RNA Helicases