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Protein & Peptide Letters


ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

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

Author(s): Jing-Jin Ding, Jin-ku Bao, De-Yu Zhu, Ying Zhang and Da-Cheng Wang

Volume 15, Issue 4, 2008

Page: [411 - 414] Pages: 4

DOI: 10.2174/092986608784246551

Price: $65


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.

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

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