ArticleActa crystallographica. Section F, Structural biology and crystallization communications2011
Cloning, expression, purification, crystallization and preliminary X-ray studies of the mannose-binding lectin domain of MSMEG_3662 from Mycobacterium smegmatis.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Glycan-mediated adhesion mechanisms in antibiotic-resistant bacteria.BBA advances · 2025Article
- LlpB represents a second subclass of lectin-like bacteriocins.Microbial biotechnology · 2019Article
- Structural studies on a non-toxic homologue of type II RIPs from bitter gourd: Molecular basis of non-toxicity, conformational selection and glycan structure.Journal of biosciences · 2015Article
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4 authors.
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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.
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