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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