Crystallization and preliminary crystallographic analysis of an Ig-domain-encompassing fragment of the giant adhesion protein SiiE from Salmonella enterica

DC FieldValueLanguage
dc.contributor.authorSturm, Karina U.
dc.contributor.authorGriessl, Martin H.
dc.contributor.authorWagner, Carolin
dc.contributor.authorDeiwick, Joerg
dc.contributor.authorHensel, Michael
dc.contributor.authorMuller, Yves A.
dc.date.accessioned2021-12-23T16:08:40Z-
dc.date.available2021-12-23T16:08:40Z-
dc.date.issued2011
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/8390-
dc.description.abstractSalmonella infections can be life-threatening. SiiE is a giant adhesion molecule of 5559 amino acids that is encoded in Salmonella pathogenicity island 4 (SPI4) and that promotes the initial contact between the pathogen and polarized epithelial cells in the intestine of the host. Starting from an engineered deletion version of SiiE (mini-SiiE; 97 kDa), limited proteolysis was used to reproducibly generate a 30 kDa fragment that readily crystallized. Mass spectrometry hints that this fragment spans the predicted Ig domains 50-52 of SiiE. Crystals of both native and selenomethionine-labelled protein could be obtained in space group C2 and diffraction data were recorded to a resolution of 1.85 angstrom.
dc.description.sponsorshipDeutsche ForschungsgemeinschaftGerman Research Foundation (DFG) [SFB 796]; We would like to thank Uwe Muller and Manfred Weiss at the BESSY synchrotron (Berlin, Germany) for help with data collection and Madhumati Sevvana for help with phasing. We thank Mattes Schulze and Rainer Buchholz from the Lehrstuhl fur Biover-fahrenstechnik, University Erlangen-Nuremberg for help with the initial mass-spectrometric analysis and Stefan Walter from the Division of Microbiology, University of Osnabruck for help with LC-ESI-MS. This work was supported by the Deutsche Forschungsgemeinschaft within the framework of SFB 796 (Teilprojekt Z).
dc.language.isoen
dc.publisherINT UNION CRYSTALLOGRAPHY
dc.relation.ispartofACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
dc.subjectBiochemical Research Methods
dc.subjectBiochemistry & Molecular Biology
dc.subjectBiophysics
dc.subjectCrystallography
dc.subjectNON-FIMBRIAL ADHESIN
dc.subjectSECRETION SYSTEM
dc.titleCrystallization and preliminary crystallographic analysis of an Ig-domain-encompassing fragment of the giant adhesion protein SiiE from Salmonella enterica
dc.typejournal article
dc.identifier.doi10.1107/S1744309111032039
dc.identifier.isiISI:000296793300012
dc.description.volume67
dc.description.issue11
dc.description.startpage1371
dc.description.endpage1374
dc.contributor.orcid0000-0003-0519-8928
dc.contributor.researcheridR-5397-2016
dc.identifier.eissn2053230X
dc.publisher.place2 ABBEY SQ, CHESTER, CH1 2HU, ENGLAND
dcterms.isPartOf.abbreviationActa Crystallogr. F-Struct. Biol. Commun.
dcterms.oaStatusGreen Published
crisitem.author.deptFB 05 - Biologie/Chemie-
crisitem.author.deptidfb05-
crisitem.author.orcid0000-0001-6604-6253-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.netidHeMi480-
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