Overexpression, crystallization and preliminary X-ray crystallographic analysis of the RNA polymerase domain of primase from Streptococcus mutans strain UA159.
Primase is the enzyme that synthesizes RNA primers on single-stranded DNA during normal DNA replication. In this study, the catalytic core domain of primase from Streptococcus mutans UA159 was overexpressed in Escherichia coli, purified and crystallized. Diffraction data were collected to 1.60 Å resolution using a synchrotron-radiation source. The crystal belonged to space group P4(1) or P4(3), with unit-cell parameters a = b = 52.63, c = 110.31 Å. The asymmetric unit is likely to contain one molecule, with a corresponding V(M) of 1.77 Å(3) Da(-1) and a solvent content of 30.7%.
Department of Chemistry, Konkuk University, Hwayang-dong, Gwangjin-gu, Seoul 143-701, Republic of Korea.
Dong-Won
DW
Im
Tae-O
TO
Kim
Ha Yun
HY
Jung
Ji Eun
JE
Oh
Se Jin
SJ
Lee
Yong-Seok
YS
Heo
D003460:Crystallization; D018360:Crystallography, X-Ray; D019915:DNA Primase / Q000737:chemistry*; D017434:Protein Structure, Tertiary; D013295:Streptococcus mutans / Q000201:enzymology*
D019915:DNA Primase