首页> 美国卫生研究院文献>Acta Crystallographica Section F: Structural Biology and Crystallization Communications >Overexpression crystallization and preliminary X-­ray crystallographic analysis of the RNA polymerase domain of primase from Streptococcus mutans strain UA159
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Overexpression crystallization and preliminary X-­ray crystallographic analysis of the RNA polymerase domain of primase from Streptococcus mutans strain UA159

机译:变形链球菌UA159菌株的primase的RNA聚合酶结构域的过表达结晶和初步X射线晶体学分析

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摘要

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 P41 or P43, 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 Å3 Da−1 and a solvent content of 30.7%.
机译:Primase是在正常DNA复制过程中在单链DNA上合成RNA引物的酶。在这项研究中,来自变形链球菌UA159的primase的催化核心结构域在大肠杆菌中过表达,纯化和结晶。使用同步辐射源将衍射数据收集到1.60Å分辨率。该晶体属于空间群P41或P43,单位晶胞参数a = b = 52.63,c = 110.31Å。不对称单元可能包含一个分子,相应的V M为1.77Å 3 Da -1 ,溶剂含量为30.7%。

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