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  • Title: Crystallization and preliminary structural studies of Scilla campanulata lectin complexed with alpha1-6 mannobiose.
    Author: Wright LM, Wood SD, Reynolds CD, Rizkallah PJ, Allen AK.
    Journal: Acta Crystallogr D Biol Crystallogr; 1998 Jan 01; 54(Pt 1):90-2. PubMed ID: 9761821.
    Abstract:
    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.
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