Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of the structural domain of the nucleocapsid N protein from porcine reproductive and respiratory syndrome virus (PRRSV)

被引：5

作者：

Doan, DNP ^{[1
]}

Dokland, T ^{[1
]}

机构：

[1] Natl Univ Singapore, Inst Mol & Cell Biol, Singapore 117609, Singapore

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 2003年 / 59卷

关键词：

D O I：

10.1107/S0907444903012721

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The structural domain of the PRRSV nucleocapsid N protein was overexpressed in Escherichia coli and purified to homogeneity. Crystals of the expressed protein, designated His-NDelta(57), were obtained by hanging-drop vapour diffusion using PEG 3350 as precipitant at pH 6.5. A native data set from a frozen crystal was collected to 2.7 Angstrom resolution using synchrotron radiation. The crystals belong to space group P3(1)21 or P3(2)21, with unit-cell parameters a = 44.41, c = 125.05, and contain a dimer in the asymmetric unit.

引用

页码：1504 / 1506

页数：3

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