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

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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.

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

Document Type: Research Article

Affiliations: Institute of Biostructures and Bioimaging, CNR, Via Mezzocannone, n. 16. I-80134 Napoli, Italy.

Publication date: 2007-04-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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