title: Crystallization of domains involved in self-assembly of the S-layer protein SbsC.
abstract: The Gram-positive bacterium Geobacillus stearothermophilus ATCC 12980 is completely covered with a two-dimensional crystalline monolayer composed of the S-layer protein SbsC. In order to complete the structure of the full-length protein, additional soluble constructs containing the crucial domains for self-assembly have been successfully cloned, expressed and purified. Crystals obtained from three different recombinant constructs yielded diffraction to 3.4, 2.8 and 1.5 Å resolution. Native data have been collected.
authors.affiliation: Institute of Molecular Biosciences, Karl-Franzens University Graz, Humboldtstrasse 50, 8010 Graz, Austria.
authors.forename: Anđela
authors.initials: A
authors.lastname: Ðordić
authors.forename: Eva M
authors.initials: EM
authors.lastname: Egelseer
authors.forename: Manfred
authors.initials: M
authors.lastname: Tesarz
authors.forename: Uwe B
authors.initials: UB
authors.lastname: Sleytr
authors.forename: Walter
authors.initials: W
authors.lastname: Keller
authors.forename: Tea
authors.initials: T
authors.lastname: Pavkov-Keller
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D002473:Cell Wall / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray; D001411:Geobacillus stearothermophilus / Q000378:metabolism*; D008562:Membrane Glycoproteins / Q000737:chemistry* / Q000378:metabolism; D017434:Protein Structure, Tertiary
chemical_list: D001426:Bacterial Proteins; D008562:Membrane Glycoproteins; C055764:S-layer proteins