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. 2006 Sep;44(9):3134–3138. doi: 10.1128/JCM.00693-06

FIG. 1.

FIG. 1.

Expression and purification of recombinant NiV-N protein. A recombinant plasmid containing the full-length Nipah virus N gene was transformed into E. coli XL1-Blue and induced with IPTG. E. coli cells were collected and dissolved in 10 mM PBS (pH 7.5)-500 mM NaCl. After sonication, the E. coli cell lysate was centrifuged and the recombinant protein was purified from the supernatant by use of a Talon immobilized metal affinity column. The E. coli cell lysate and purified recombinant protein were analyzed in a 10% SDS-PAGE gel and revealed with Coomassie brilliant blue staining. Lane M, protein marker (SDS-7B); lane 1, supernatant of sonicated E. coli cell lysate after centrifugation; lane 2, pellet of sonicated E. coli cell lysate; lane 3, purified recombinant protein.