Crystallization and X-ray diffraction analysis of chondroitin lyase from baculovirus: Envelope protein ODV-E66

Yoshirou Kawaguchi, Nobuo Sugiura, Momo Onishi, Koji Kimata, Makoto Kimura, Yoshimitu Kakuta

Research output: Contribution to journalArticlepeer-review

4 Citations (Scopus)

Abstract

Baculovirus envelope protein ODV-E66 (67-704), in which the N-terminal 66 amino acids are truncated, is a chondroitin lyase. It digests chondroitin and chondroitin 6-sulfate efficiently, but does not digest chondroitin 4-sulfate. This unique characteristic is useful for the preparation of specific chondroitin oligosaccharides and for investigation of the mechanism of baculovirus infection. ODV-E66 (67-704) was crystallized; the crystal diffracted to 1.8 Å resolution and belonged to space group P62 or P64, with unit-cell parameters a = b = 113.5, c = 101.5 Å. One molecule is assumed to be present per asymmetric unit, which gives a Matthews coefficient of 2.54 Å 3 Da -1.

Original languageEnglish
Pages (from-to)190-192
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume68
Issue number2
DOIs
Publication statusPublished - Feb 2012

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

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