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Kurinov, I.V. et al.

Kurinov, Mao, Irvin, Uckun,

X-ray crystallographic analysis of pokeweed antiviral protein-II after reductive methylation of lysine residues.

Pokeweed antiviral protein II ( PAP-II) is a naturally occurring protein isolated from early summer leaves of the pokeweed plant (Phytolacca americana). PAP-II belongs to a family of ribosome-inactivating proteins which catalytically deadenylate ribosomal and viral RNA. The chemical modification of PAP-II by reductive methylation of its lysine residues significantly improved the crystal quality for X-ray diffraction studies. Hexagonal crystals of the modified PAP-II, with unit cell parameters a = b = 92.51 A, c = 79.05 A, were obtained using 1.8 M Na/K phosphate as the precipitant. These crystals contained one enzyme molecule per asymmetric unit and diffracted up to 2.4 A, when exposed to a synchroton source.[1]

References

X-ray crystallographic analysis of pokeweed antiviral protein-II after reductive methylation of lysine residues. Kurinov, I.V., Mao, C., Irvin, J.D., Uckun, F.M. Biochem. Biophys. Res. Commun. (2000) [Pubmed]

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