Crystallization and preliminary x-ray diffraction analysis of a novel mannose-binding lectin with antiretroviral properties from Polygonatum cyrtonema hua.
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 A resolution and belong to space group P2(1), with unit-cell parameters of a=39.308 A, b=48.317 A, c=112.221 A, and beta=90.12 degrees . 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.
Ding
Jing-Jin
JJ
National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, People's Republic of China.
Bao
Jin-Ku
JK
Zhu
De-Yu
DY
Zhang
Ying
Y
Wang
Da-Cheng
DC
D000595:Amino Acid Sequence; D044966:Anti-Retroviral Agents / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray; D008969:Molecular Sequence Data; D037121:Plant Lectins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D031384:Polygonatum / Q000737:chemistry*; D016415:Sequence Alignment; D014961:X-Ray Diffraction
D044966:Anti-Retroviral Agents; D037121:Plant Lectins