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Overexpression, crystallization and preliminary X-ray crystallographic analysis of the RNA polymerase domain of primase from Streptococcus mutans strain UA159.

ABSTRACT: 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%.

SUBMITTER: Im DW

PROVIDER: S-EPMC3253846 | biostudies-literature | 2012 Jan

REPOSITORIES: biostudies-literature

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Overexpression, crystallization and preliminary X-ray crystallographic analysis of the RNA polymerase domain of primase from Streptococcus mutans strain UA159.

Im Dong-Won DW Kim Tae-O TO Jung Ha Yun HY Oh Ji Eun JE Lee Se Jin SJ Heo Yong-Seok YS

Acta crystallographica. Section F, Structural biology and crystallization communications 20111224 Pt 1

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 mo ...[more]

PMID: 22232183

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