Crystallization and preliminary crystallographic analyses of pokeweed antiviral protein from seeds

Hong Min Li, Zong Hao Zeng, Zhong Hu, D. A.Cheng Wang

Research output: Contribution to journalArticlepeer-review

8 Scopus citations

Abstract

Pokeweed antiviral protein from seeds (PAP-S) is a ribosome inactivating protein which has lowest toxicity and highest inhibition activity as opposed to other pokeweed antiviral proteins and its three potential glycosylation sites (10, 44, 255) were shown to bind to N-acetylglucosamine. Good quality crystals of PAP-S were grown at high protein concentration (100 mg ml-1) and high temperature (306 K). The crystals have space group I222 and cell parameters a = 78.7, b = 85.2 and c = 93.0 Å. An X-ray diffraction data set with resolution up to 1.8 Å was collected. This high-resolution data will help to locate the sugars bound to the protein and provide accurate structural data for understanding structure-function relationships of PAP-S.

Original languageEnglish (US)
Pages (from-to)137-139
Number of pages3
JournalActa Crystallographica Section D: Biological Crystallography
Volume54
Issue number1
DOIs
StatePublished - Jan 1 1998
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology

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