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.
Wright
L M
LM
School of Biomolecular Sciences, Liverpool John Moores University, Byrom Street, Liverpool L3 3AF, England. bmslwril@livjm.ac.uk
Wood
S D
SD
Reynolds
C D
CD
Rizkallah
P J
PJ
Allen
A K
AK
D003460:Crystallization; D037102:Lectins / Q000737:chemistry*; D008351:Mannans / Q000737:chemistry*; D012984:Software; D017356:Synchrotrons; D014961:X-Ray Diffraction
D037102:Lectins; D008351:Mannans; C014647:mannobiose