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

Autor(en): Sturm, Karina U.
Griessl, Martin H.
Wagner, Carolin
Deiwick, Joerg
Hensel, Michael 
Muller, Yves A.
Stichwörter: Biochemical Research Methods; Biochemistry & Molecular Biology; Biophysics; Crystallography; NON-FIMBRIAL ADHESIN; SECRETION SYSTEM
Erscheinungsdatum: 2011
Herausgeber: INT UNION CRYSTALLOGRAPHY
Journal: ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
Volumen: 67
Ausgabe: 11
Startseite: 1371
Seitenende: 1374
Zusammenfassung: 
Salmonella 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.
DOI: 10.1107/S1744309111032039

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