{"refrec":{"BRefID":280922,"RR":"<b>Agapay, R.C.; Savvides, S.N.; Van Driessche, G.; Devreese, B.; Van Beeumen, J.; Jongejan, J.A.; Hagen, W.R.</b> (2005). Expression, purification, crystallization and preliminary crystallographic analysis of a stand-alone RAM domain with hydrolytic activity from the hyperthermophile <i>Pyrococcus furiosus</i>. <i>Acta Crystallographica Section F-Structural Biology Communications 61</i>: 914-916. <a href=\"http://dx.doi.org/10.1107/S1744309105028393\" target=\"_blank\">dx.doi.org/10.1107/S1744309105028393</a>","BEntID":272941,"PublicFlag":1,"CheckedFlag":1,"wosflag":1,"vabbflag":0,"RefStringPartII":". <i>Acta Crystallographica Section F-Structural Biology Communications 61</i>: 914-916. <a href=\"https://dx.doi.org/10.1107/S1744309105028393\" target=\"_blank\">https://dx.doi.org/10.1107/S1744309105028393</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Agapay, R.C.; Savvides, S.N.; Van Driessche, G.; Devreese, B.; Van Beeumen, J.; Jongejan, J.A.; Hagen, W.R.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Agapay, R.C. <i>et al.</i>","Englishabstract":"The RAM domain is one of several ligand-binding modules present in prokaryotes that are presumed to regulate the transcription of specific genes. To date, no hydrolytic activity has been reported for such modules. Curiously, a stand-alone RAM domain in <i>Pyrococcus furiosus</i> was isolated during a screen for hydrolytic activity against chromogenic esters. The gene encoding this protein was cloned and expressed in <i>Escherichia coli</i> and crystallized after a single purification step. X-ray diffraction data from the crystals were obtained to a resolution of 2.8 Å using a conventional X-ray source. The cocrystallization of the recombinant protein with 1,2-epoxy-3-(4-nitrophenoxy)propane (EPNP) and phenylmethylsulfonyl fluoride (PMSF) produced crystals that yielded data to 2.2 and 2.8 Å, respectively, using synchrotron radiation. Both the untreated and EPNP-treated crystals crystallize isomorphously in space group <i>C</i>2 and contain three dimers in the asymmetric unit. The PMSF-treated crystals also belong to this space group and have almost identical packing density, but show dramatically different unit-cell parameters.","AbstractOtherLang":null,"BibLvlCode":"AS","StandardTitle":"Expression, purification, crystallization and preliminary crystallographic analysis of a stand-alone RAM domain with hydrolytic activity from the hyperthermophile <i>Pyrococcus furiosus</i>","OrigTitleLangCode":"en","OrigTitleLangCodeExtended":"eng","OrigTitleLangID":15,"DateLastModified":{"date":"2024-12-10 01:33:17.368041","timezone_type":1,"timezone":"+01:00"},"UserAccessRight":null,"UserAccID":null,"AuthorKeywords":null,"OtherDescriptors":null,"Notes":null,"AnaPub":2005,"MonPub":null,"DateUpdate":"2016-12-02","DateCreate":"2016-10-09","SecASFANote":null,"ConfID":null,"PeerRev":1,"VlizCoreFlag":1,"WoScode":"WOS:000232354300013","VABBcode":null,"OpenAcc":0,"DOI":"10.1107/S1744309105028393"},"refs":null,"anarec":{"AnaID":280922,"PubliDate":2005,"Pagination":"914-916","XtraPublOfAnaID":null,"ISBN":null,"Volume":"61","Issue":null,"BRefMon":null,"BRefMonRR":null,"BRefXtra":null,"BRefXtraRR":null,"SerBRefID":262454,"SerRR":"Acta Crystallographica Section F-Structural Biology Communications. 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