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 Iron-sulfur cluster coordination in the [FeFe]-hydrogenase H cluster biosynthetic factor HydF. Iron-sulfur cluster coordination in the [FeFe]-hydrogenase H cluster biosynthetic factor HydF. FEBS Lett. (0014-5793) 2012 Joshi N., Shepard EM., Byer AS., Swanson KD., Broderick JB., Peters JW. in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Joshi N., Shepard EM., Byer AS., Swanson KD., Broderick JB., Peters JW. FEBS Lett. (0014-5793) 2012 q97ij0_cloab CA_C1651 protein protein cloab Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) MNELNSTPKGERLHIALFGKTNVGKSSVINALTSQEIALVSNVKGTTTDPVYKAMELLPLGPVMLIDTAGLDDISDLGELRRGKTLEVLSKTDVAILVFDVESGITEYDKNIYSLLLEKKIPLIGVLNKIDKKDYKLEDYTSQFKIPIVPISALNNKGINNLKDELIRLAPENDDKFKIVGDLLSPGDIAVLVTPIDKAAPKGRLILPQQQTIRDILESDAIAMVTKEFELRETLDSLRKKPKIVITDSQVFLKVAADTPKDILMTSFSILMARHKGDLIELARGARAIEDLKDGDKILIAEACTHHRQSDDIGKVKIPRWLRQKTGKKLEFDFSSGFSFPPNIEDYALIVHCAGCMLNRRSMLHRIESSVKKQIPIVNYGVLIAYVQGILPRALKPFPYADRIFNQSSRN mint 15F65B92CE4201B8 q97ij0 1 HydF 2 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 2.0 direct interaction direct interaction sf2 mint Gel filtration chromatography showed that most of the variant proteins have similar tetrameric to dimeric content in comparison to wild type enzyme, indicating no substantial deviations in overall protein structure. However, C304A and C304S mutant proteins were found to contain significantly less tetrameric content (Figure S2), in line with the results presented in the structure work on the analogous mutant in Thermotoga neapolitana (C302S). q97ij0-1 1 HydF 2 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 4.0 direct interaction direct interaction sf2 mint Gel filtration chromatography showed that most of the variant proteins have similar tetrameric to dimeric content in comparison to wild type enzyme, indicating no substantial deviations in overall protein structure. However, C304A and C304S mutant proteins were found to contain significantly less tetrameric content (Figure S2), in line with the results presented in the structure work on the analogous mutant in Thermotoga neapolitana (C302S).