Crystallization and Preliminary X-Ray Diffraction Analysis of PD-L1, a Highly Glycosylated Ribosome Inactivating Protein with DNase Activity

Alessia      Ruggiero; Angela      Chambery; Antimo      Di Maro; Antonietta      Mastroianni; Augusto      Parente; Rita      Berisio

Protein & Peptide Letters

Author(s): Alessia Ruggiero, Angela Chambery, Antimo Di Maro, Antonietta Mastroianni, Augusto Parente and Rita Berisio

DOI: 10.2174/092986607780363899

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Crystallization and Preliminary X-Ray Diffraction Analysis of PD-L1, a Highly Glycosylated Ribosome Inactivating Protein with DNase Activity

Page: [407 - 709] Pages: 303

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Abstract

PD-L1 is a highly glycosylated type 1 ribosome inactivating protein, from Phytolacca dioica leaves, with the peculiarity to act also as a DNase. PD-L1 has been successfully crystallized using vapour diffusion and seeding techniques. Crystals belong to the monoclinic C2 space group, with unit cell dimensions a=161.01, b=34.73, c=120.63 Å, β=127.99 . Two molecules are present in the asymmetric unit. Phase determination has been achieved using molecular replacement.

Keywords: Ribosome inactivating protein, Phytolacca dioica, crystallization, glycosylation, seeding, X-ray

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