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Crystallization and biochemical characterization of an archaeal lectin from Methanococcus voltae A3.

ABSTRACT: A lectin from Methanococcus voltae A3 has been cloned, expressed, purified and characterized. The lectin appears to be specific for complex sugars. The protein crystallized in a tetragonal space group, with around 16 subunits in the asymmetric unit. Sequence comparisons indicate the lectin to have a ?-prism I fold, with poor homology to lectins of known three-dimensional structure.

SUBMITTER: Sivaji N 

PROVIDER: S-EPMC5417321 | biostudies-literature | 2017 May

REPOSITORIES: biostudies-literature

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Crystallization and biochemical characterization of an archaeal lectin from Methanococcus voltae A3.

Sivaji N N   Abhinav K V KV   Vijayan M M  

Acta crystallographica. Section F, Structural biology communications 20170428 Pt 5

A lectin from Methanococcus voltae A3 has been cloned, expressed, purified and characterized. The lectin appears to be specific for complex sugars. The protein crystallized in a tetragonal space group, with around 16 subunits in the asymmetric unit. Sequence comparisons indicate the lectin to have a β-prism I fold, with poor homology to lectins of known three-dimensional structure. ...[more]

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