Crystallization and preliminary X-ray diffraction analysis of PD-L1, a highly glycosylated ribosome inactivating protein with DNase activity

Protein Pept Lett. 2007;14(4):407-9. doi: 10.2174/092986607780363899.

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 A, beta=127.99 degrees . Two molecules are present in the asymmetric unit. Phase determination has been achieved using molecular replacement.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallization
  • Crystallography, X-Ray
  • Deoxyribonucleases / chemistry*
  • Deoxyribonucleases / isolation & purification*
  • N-Glycosyl Hydrolases / chemistry*
  • N-Glycosyl Hydrolases / isolation & purification*
  • Phytolacca / chemistry*
  • Plant Leaves / chemistry
  • Plant Proteins / chemistry*
  • Plant Proteins / isolation & purification*
  • Ribosome Inactivating Proteins
  • Ribosome Inactivating Proteins, Type 1

Substances

  • Plant Proteins
  • Ribosome Inactivating Proteins, Type 1
  • Deoxyribonucleases
  • N-Glycosyl Hydrolases
  • Ribosome Inactivating Proteins
  • pokeweed antiviral protein