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).

Academic Article

Abstract

  • 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 A 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.
  • Authors

    Keywords

  • Cloning, Molecular, Crystallization, Crystallography, X-Ray, DNA, Complementary, Dimerization, Escherichia coli, Histidine, Hydrogen-Ion Concentration, Nucleocapsid Proteins, Porcine respiratory and reproductive syndrome virus, Protein Structure, Tertiary, X-Ray Diffraction
  • Digital Object Identifier (doi)

    Author List

  • Doan DNP; Dokland T
  • Start Page

  • 1504
  • End Page

  • 1506
  • Volume

  • 59
  • Issue

  • Pt 8