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Crystallization and Preliminary X-Ray Diffraction Analysis of a Novel Mannose-Binding Lectin with Antiretroviral Properties from Polygonatum cyrtonema Hua

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A novel antiretroviral protein Polygonatum cyrtonema lectin (PCL) belonging to the monocot mannose-binding lectin (MMBL) superfamily has been crystallized using hanging-drop vapor-diffusion method. The crystals diffract to 2.0 Å resolution and belong to space group P21, with unit-cell parameters of a=39.308 Å, b=48.317 Å, c=112.221 Å, and β=90.12° . Preliminary analysis indicates that the asymmetric unit contains four PCL molecules with a solvent content of about 45%. A set of X-ray data has been collected for the crystal structure determination.





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Keywords: PCL; Polygonatum cyrtonema Hua; crystallization; monocot mannose-binding lectin; preliminary X-ray diffraction analysis

Document Type: Research Article

Publication date: 2008-05-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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