Crystallization and preliminary structural studies of Scilla campanulata lectin complexed with alpha1-6 mannobiose.
Recent work has shown that Scilla campanulata agglutinin from bluebell bulbs has a strong affinity for alpha(1,3)- and alpha(1,6)-linked mannosyl residues and possesses moderate antiretroviral activity. This lectin has been crystallized by the hanging-drop method of vapour diffusion complexed with the disaccharide mannose-alpha1,6-D-mannose. The crystals are in the space group P21212 with unit-cell dimensions a = 70.63, b = 92.79 and c = 47.25 A, and with a dimer in the asymmetric unit. The crystals diffract X-rays to beyond 1.5 A resolution at 277 K and are stable in an X-ray beam. Data to 1.6 A resolution have been collected using a MAR image-plate system at a synchrotron source and the structure of the complex has been solved by the molecular replacement method.
School of Biomolecular Sciences, Liverpool John Moores University, Byrom Street, Liverpool L3 3AF, England. bmslwril@livjm.ac.uk
L M
LM
Wright
S D
SD
Wood
C D
CD
Reynolds
P J
PJ
Rizkallah
A K
AK
Allen
D003460:Crystallization; D037102:Lectins / Q000737:chemistry*; D008351:Mannans / Q000737:chemistry*; D012984:Software; D017356:Synchrotrons; D014961:X-Ray Diffraction
D037102:Lectins; D008351:Mannans; C014647:mannobiose