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

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

Volume: 14 Issue: 4

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

Affiliation:

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

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.

Cite this article as:

Ruggiero Alessia, Chambery Angela, Di Maro Antimo, Mastroianni Antonietta, Parente Augusto and Berisio Rita, Crystallization and Preliminary X-Ray Diffraction Analysis of PD-L1, a Highly Glycosylated Ribosome Inactivating Protein with DNase Activity, Protein & Peptide Letters 2007; 14 (4) . https://dx.doi.org/10.2174/092986607780363899