Cloning, expression, and purification of the virulence-associated protein D from Xylella fastidiosa
In this study, an efficient expression system, based on the pET32Xa/LIC vector, for producing
a Xylella fastidiosa virulence-associated protein D, found to have a strong similarity to
Riemerella anatipestifer and Actinobacillus actinomycetencomitans VapD protein, is
presented. The protein has a molecular mass of 17.637 Da and a calculated pI of 5.49. The
selected XFa0052 gene was cloned in the pET32Xa/LIC vector and the plasmid was
transformed into Escherichia coli BL21 (DE3) strain at 37° C, with an induction time of 2h …
a Xylella fastidiosa virulence-associated protein D, found to have a strong similarity to
Riemerella anatipestifer and Actinobacillus actinomycetencomitans VapD protein, is
presented. The protein has a molecular mass of 17.637 Da and a calculated pI of 5.49. The
selected XFa0052 gene was cloned in the pET32Xa/LIC vector and the plasmid was
transformed into Escherichia coli BL21 (DE3) strain at 37° C, with an induction time of 2h …
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