TY - JOUR
T1 - Crystallization and X-ray diffraction analysis of chondroitin lyase from baculovirus
T2 - Envelope protein ODV-E66
AU - Kawaguchi, Yoshirou
AU - Sugiura, Nobuo
AU - Onishi, Momo
AU - Kimata, Koji
AU - Kimura, Makoto
AU - Kakuta, Yoshimitu
PY - 2012/2
Y1 - 2012/2
N2 - 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.
AB - 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.
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U2 - 10.1107/S1744309111053164
DO - 10.1107/S1744309111053164
M3 - Article
C2 - 22297996
AN - SCOPUS:84856897469
SN - 1744-3091
VL - 68
SP - 190
EP - 192
JO - Acta Crystallographica Section F:Structural Biology Communications
JF - Acta Crystallographica Section F:Structural Biology Communications
IS - 2
ER -