Scilla campanulata agglutinin crystallized in complex with the trimannoside alpha-D-man-(1-->6)-[alpha-D-man-(1-->3)]-alpha-D-Man.
Acta Crystallogr D Biol Crystallogr
; 54(Pt 4): 665-7, 1998 Jul 01.
Article
em En
| MEDLINE
| ID: mdl-9761869
ABSTRACT
The monocot mannose-specific lectin, Scilla campanulata agglutinin (SCA), from bluebell bulbs has a strong affinity for alpha1,3- and alpha1,6-linked mannosyl residues. SCA has been co-crystallized with the trisaccharide alpha-D-mannopyranosyl-(1-->6)-alpha-D-mannopyranosyl-(1-->3)-alpha-D -mannopyranoside ¿alpha-D-Man-(1-->6)-[alpha-D-Man-(1-->3)]-alpha-D-Man¿, the core structure of biantennary N-linked oligosaccharides. Crystals of the complex were obtained by the hanging-drop vapour-diffusion technique. A complete data set to 2.5 A resolution has been collected at 100 K, using a MAR image-plate system at a synchrotron source, from crystals which belong to the space group C2 with unit-cell dimensions a = 99.38, b = 119.86, c = 77.10 A and beta = 105.56 degrees. Use of a CCD detector with cryo-cooled crystals improved the resolution to 2.3 A. A molecular replacement solution, with the 2.5 A data set, using the native SCA as a search model was obtained, with six subunits per asymmetric unit.
Buscar no Google
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas de Plantas
/
Trissacarídeos
/
Aglutininas
Idioma:
En
Revista:
Acta Crystallogr D Biol Crystallogr
Ano de publicação:
1998
Tipo de documento:
Article