Open AccessCrystallization and X‐ray diffraction analysis of chondroitin lyase from baculovirus: envelope protein ODV‐E66
Author(s) -
Kawaguchi Yoshirou,
Sugiura Nobuo,
Onishi Momo,
Kimata Koji,
Kimura Makoto,
Kakuta Yoshimitu
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111053164
Subject(s) - crystallization , envelope (radar) , materials science , diffraction , crystallography , chemistry , physics , optics , computer science , telecommunications , radar , organic chemistry
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 P 6 2 or P 6 4 , 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 .