X-Ray Crystallographic Analysis of Pokeweed Antiviral Protein-II after Reductive Methylation of Lysine Residues

Autor: Kurinov, I. V., Mao, C., Irvin, J. D., Uckun, F. M.
Zdroj: Biochemical and Biophysical Research Communications; August 28, 2000, Vol. 275 Issue: 2 p549-552, 4p
Abstrakt: 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.
Databáze: Supplemental Index