X-Ray Crystallographic Analysis of Pokeweed Antiviral Protein-II after Reductive Methylation of Lysine Residues
Authors: Kurinov I.V.1; Mao C.1; Irvin J.D.2; Uckun F.M.1
Source: Biochemical and Biophysical Research Communications, Volume 275, Number 2, August 2000 , pp. 549-552(4)
Publisher: Academic Press
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Abstract:
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 Å, c = 79.05 Å, 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 Å, when exposed to a synchroton source. Copyright 2000 Academic Press.
Keywords: pokeweed antiviral protein; reductive methylation; crystallization; X-ray diffraction
Language: English
Document Type: Research article
Affiliations: 1: Department of Biotherapy, Parker Hughes Institute, Roseville, Minnesota, 55113 2: Department of Chemistry, SouthWest Texas State University, San Marcos, Texas, 78666
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