MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it http://mint.bio.uniroma2.it/mint anonymous-2013k-1 Biochemical and structural characterisation of a novel bacterial manganese-dependent hydroxynitrile lyase in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Hajnal I., Lyskowski A., Hanefeld U., Gruber K., Schwab H., Steiner K. kerstin.steiner@acib.at FEBS J. (1742-464X) 2013 Only protein-protein interactions imex curation e8wyn5_gratm AciX9_0562 protein protein gratm Granulicella tundricola (strain ATCC BAA-1859 / DSM 23138 / MP5ACTX9) MEIKRVGSQASGKGPADWFTGTVRIDPLFQAPDPALVAGASVTFEPGARTAWHTHPLGQTLIVTAGCGWAQREGGAVEEIHPGDVVWFSPGEKHWHGAAPTTAMTHLAIQERLDGKAVDWMEHVTDEQYRR e8wyn5-e8wyn5 1436083 n/a GtHNL 1436084 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified ecoli Escherichia coli (strain K12) Stoichiometry: 4.0 direct interaction direct interaction false false false t2, st2, f5, f6 The His-tagged protein was purified efficiently using Ni SepharoseTM 6 Fast Flow resin and subsequent size-exclusion chromatography as described before [19]. Protein crystals diffracted to ~2.5 Å and contained two homotetramers in the asymmetric unit (Fig. 5a).