Crystallization and preliminary X-ray diffraction analysis of PD-L1, a highly glycosylated ribosome inactivating protein with DNase activity.
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 A, beta=127.99 degrees . Two molecules are present in the asymmetric unit. Phase determination has been achieved using molecular replacement.
Ruggiero
Alessia
A
Istituto di Biostrutture e Bioimmagini, CNR, I-80134 Napoli, Italy.
Chambery
Angela
A
Di Maro
Antimo
A
Mastroianni
Antonietta
A
Parente
Augusto
A
Berisio
Rita
R
D003460:Crystallization; D018360:Crystallography, X-Ray; D003851:Deoxyribonucleases / Q000737:chemistry* / Q000302:isolation & purification*; D009699:N-Glycosyl Hydrolases / Q000737:chemistry* / Q000302:isolation & purification*; D029603:Phytolacca / Q000737:chemistry*; D018515:Plant Leaves / Q000737:chemistry; D010940:Plant Proteins / Q000737:chemistry* / Q000302:isolation & purification*; D054788:Ribosome Inactivating Proteins; D054789:Ribosome Inactivating Proteins, Type 1
D010940:Plant Proteins; D054789:Ribosome Inactivating Proteins, Type 1; D003851:Deoxyribonucleases; D009699:N-Glycosyl Hydrolases; D054788:Ribosome Inactivating Proteins; C024275:pokeweed antiviral protein