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

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

Volume: 15 Issue: 4

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

Affiliation:

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

Abstract: 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.

Cite this article as:

Ding Jing-Jin, Bao Jin-ku, Zhu De-Yu, Zhang Ying and Wang Da-Cheng, Crystallization and Preliminary X-Ray Diffraction Analysis of a Novel Mannose-Binding Lectin with Antiretroviral Properties from Polygonatum cyrtonema Hua, Protein & Peptide Letters 2008; 15 (4) . https://dx.doi.org/10.2174/092986608784246551