title: Cloning, expression, purification, crystallization and preliminary X-ray studies of the mannose-binding lectin domain of MSMEG_3662 from Mycobacterium smegmatis.
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.
authors.affiliation: Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India.
authors.forename: Dhabaleswar
authors.initials: D
authors.lastname: Patra
authors.forename: Alok
authors.initials: A
authors.lastname: Sharma
authors.forename: Divya
authors.initials: D
authors.lastname: Chandran
authors.forename: Mamannamana
authors.initials: M
authors.lastname: Vijayan
mesh_terms: D001665:Binding Sites; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D037601:Mannose-Binding Lectin / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D020102:Mycobacterium smegmatis / Q000737:chemistry*
chemical_list: D037601:Mannose-Binding Lectin