title: 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).
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.affiliation: Institute of Molecular and Cell Biology, 30 Medical Drive, Singapore 117609, Singapore. doan@imcb.nus.edu.sg
authors.forename: Danny N P
authors.initials: DN
authors.lastname: Doan
authors.forename: Terje
authors.initials: T
authors.lastname: Dokland
mesh_terms: D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D018076:DNA, Complementary / Q000378:metabolism; D019281:Dimerization; D004926:Escherichia coli / Q000378:metabolism; D006639:Histidine / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D019590:Nucleocapsid Proteins / Q000737:chemistry*; D019316:Porcine respiratory and reproductive syndrome virus / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D014961:X-Ray Diffraction
chemical_list: D018076:DNA, Complementary; D019590:Nucleocapsid Proteins; D006639:Histidine