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 byrne-2014-1 Molecular architecture of the HerA-NurA DNA double-strand break resection complex. in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column weight by staining molecular weight estimation by staining weight by staining Byrne R.T., Schuller J.M., Unverdorben P., Förster F., Hopfner K.P. foerster@biochem.mpg.de; hopfner@genzentrum FEBS Lett. (0014-5793) 2014 Only protein-protein interactions imex curation byrne-2014-2 Molecular architecture of the HerA-NurA DNA double-strand break resection complex. in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Byrne R.T., Schuller J.M., Unverdorben P., Förster F., Hopfner K.P. foerster@biochem.mpg.de; hopfner@genzentrum FEBS Lett. (0014-5793) 2014 Only protein-protein interactions imex curation byrne-2014-3 Molecular architecture of the HerA-NurA DNA double-strand break resection complex. in vitro In vitro electron microscopy electron microscopy Electron crystallography Electron cryomicroscopy Electron crystallography Electron cryomicroscopy predetermined predetermined participant predetermined Byrne R.T., Schuller J.M., Unverdorben P., Förster F., Hopfner K.P. foerster@biochem.mpg.de; hopfner@genzentrum FEBS Lett. (0014-5793) 2014 Only protein-protein interactions imex curation hera_sacs2 DNA double-strand break repair helicase HerA herA SSO2251 protein protein sulso Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) MIIGYVIGQATTQEALILAERPVRLGTYVVLEYDNVKALGLITNVTRGSPMLDDNMNDIEIVQRLKQFNNSIPVYTKAKVKMLCDMNNHFLMPDIPPFAGTPAREAEDEELKSIYSQDGQIRIGSLIGKNVEVKLNINSFARHLAILAATGSGKSNTVAVLSQRISELGGSVLIFDYHGEYYDSDIKNLNRIEPKLNPLYMTPREFSTLLEIRENAIIQYRILRRAFIKVTNGIREKLKEGQIPFSTLNSQFYELMKDELETQGNSDKKSSAKDEVLNKFEEFMDRYSNVIDLTSSDIIEKVKRGKVNVVSLTQLDEDSMDAVVSHYLRRILDSRKDFKRSKNSGLKFPIIAVIEEAHVFLSKNENTLTKYWASRIAREGRKFGVGLTIVSQRPKGLDENILSQMTNKIILKIIEPTDKKYILESSDNLSEDLAEQLSSLDVGEAIIIGKIVKLPAVVKIDMFEGKLLGSDPDMIGEWKKVEESEKIAKGFADFGTEIGD nura_sacs2 DNA double-strand break repair nuclease NurA nurA SSO2248 protein protein sulso Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) MIRKIYDKLVESHNEIKNQIYNIANYLKQEIQDKVNEYWNEYVINHEQSETCKFVAIDGGSFGRPMRIGIVYAVGAESVIGDNKGVKTLSEDGQIGIFKPGNDAQERISLLMEALELSLALRDGSKGDYILMDGSLSKKIGNKVDIQQFSDEELKLIRNVDLNGIISIKDERKMRDLLMLLNQFLVSKIIEEYDGNVLWISKVSRGRDLFGTDYPDITVLELFTEKRGFSKLIIKNIDIEKISEIPEIEVLRKMEYTTFYTRLDNGKRVIRVDIVGRVDEKIVKEIMDRLSGVSIKGYPFPLLKAHMDVRFSAMDREKIIKLVGSKLHKDIEWWPSQFY q97wg8-q97wh1-1 1778550 n/a 1778553 weight by staining molecular weight estimation by staining weight by staining unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 3.0 n/a 1778554 weight by staining molecular weight estimation by staining weight by staining unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 physical association physical association false false false f1b sf1c Mixing separately purified wild-type NurA and HerA (without fusion tags on either protein) produced a stable complex that was purified by gel filtration (Fig. 1a and b) and used for cryo-electron microscopic analysis. To confirm the stoichiometry of the complex we analyzed samples by size-exclusion chromatography coupled right-angle light scattering (SEC-RALS) in addition to densitometry of SDS–PAGE gels (Fig. S1). Both the molecular weight of 419kDa determined by SEC-RALS and the 3:1 HerA:NurA ratio determined by densitometry are consistent with the previously observed HerA–NurA complex with 6:2 stoichiometry (calculated molecular weight of 416kDa) q97wg8-q97wh1-2 1778551 n/a 1778553 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 3.0 n/a 1778554 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.0 physical association physical association false false false f1a sf1a sf1b Mixing separately purified wild-type NurA and HerA (without fusion tags on either protein) produced a stable complex that was purified by gel filtration (Fig. 1a and b) and used for cryo-electron microscopic analysis. To confirm the stoichiometry of the complex we analyzed samples by size-exclusion chromatography coupled right-angle light scattering (SEC-RALS) in addition to densitometry of SDS–PAGE gels (Fig. S1). Both the molecular weight of 419kDa determined by SEC-RALS and the 3:1 HerA:NurA ratio determined by densitometry are consistent with the previously observed HerA–NurA complex with 6:2 stoichiometry (calculated molecular weight of 416kDa) q97wg8-q97wh1-3 1778552 n/a 1778553 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 6.0 n/a 1778554 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 2.0 physical association physical association false false false f2 Mixing separately purified wild-type NurA and HerA (without fusion tags on either protein) produced a stable complex that was purified by gel filtration (Fig. 1a and b) and used for cryo-electron microscopic analysis. To confirm the stoichiometry of the complex we analyzed samples by size-exclusion chromatography coupled right-angle light scattering (SEC-RALS) in addition to densitometry of SDS–PAGE gels (Fig. S1). Both the molecular weight of 419kDa determined by SEC-RALS and the 3:1 HerA:NurA ratio determined by densitometry are consistent with the previously observed HerA–NurA complex with 6:2 stoichiometry (calculated molecular weight of 416kDa)