耻垢分枝杆菌MSMEG_3662的甘露糖结合凝集素结构域的克隆、表达、纯化、结晶及初步X射线研究。
Cloning, expression, purification, crystallization and preliminary X-ray studies of the mannose-binding lectin domain of MSMEG_3662 from Mycobacterium smegmatis.
作者信息
Patra Dhabaleswar, Sharma Alok, Chandran Divya, Vijayan Mamannamana
机构信息
Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 May 1;67(Pt 5):596-9. doi: 10.1107/S1744309111009547. Epub 2011 Apr 28.
Abstract
The mannose-binding lectin domain of MSMEG_3662 from Mycobacterium smegmatis has been cloned, expressed, purified and crystallized and the crystals have been characterized using X-ray diffraction. The Matthews coefficient suggests the possibility of two lectin domains in the triclinic cell. The amino-acid sequence of the domain indicates structural similarity to well characterized β-prism II fold lectins.
摘要
耻垢分枝杆菌中MSMEG_3662的甘露糖结合凝集素结构域已被克隆、表达、纯化并结晶，且已使用X射线衍射对晶体进行了表征。马修斯系数表明在三斜晶胞中可能存在两个凝集素结构域。该结构域的氨基酸序列显示出与已充分表征的β-棱柱II折叠凝集素的结构相似性。
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