Scilla campanulata agglutinin crystallized in complex with the trimannoside alpha-D-man-(1-->6)-[alpha-D-man-(1-->3)]-alpha-D-Man.
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.
Wright
L M
LM
School of Biomolecular Sciences, Max Perutz Building, Liverpool John Moores University, Liverpool L3 3AF, England. bmslwril@livjm.ac.uk
Rizkallah
P J
PJ
Wood
S D
SD
Reynolds
C D
CD
D000373:Agglutinins / Q000737:chemistry* / Q000302:isolation & purification; D002240:Carbohydrate Sequence; D003460:Crystallization; D018360:Crystallography, X-Ray; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000737:chemistry*; D011487:Protein Conformation; D014312:Trisaccharides / Q000737:chemistry*
D000373:Agglutinins; D010940:Plant Proteins; D014312:Trisaccharides; C115886:mannopyranosyl-1-6-(mannopyranosyl-1-3)mannopyranose