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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 ?-prism II fold lectins.

SUBMITTER: Patra D 

PROVIDER: S-EPMC3087649 | biostudies-literature | 2011 May

REPOSITORIES: biostudies-literature

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Cloning, expression, purification, crystallization and preliminary X-ray studies of the mannose-binding lectin domain of MSMEG_3662 from Mycobacterium smegmatis.

Patra Dhabaleswar D   Sharma Alok A   Chandran Divya D   Vijayan Mamannamana M  

Acta crystallographica. Section F, Structural biology and crystallization communications 20110428 Pt 5

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. ...[more]

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