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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.

SUBMITTER: Ðordic A

PROVIDER: S-EPMC3509976 | biostudies-literature | 2012 Dec

REPOSITORIES: biostudies-literature

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Crystallization of domains involved in self-assembly of the S-layer protein SbsC.

Ðordić Anđela A Egelseer Eva M EM Tesarz Manfred M Sleytr Uwe B UB Keller Walter W Pavkov-Keller Tea T

Acta crystallographica. Section F, Structural biology and crystallization communications 20121114 Pt 12

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 ...[more]

PMID: 23192035

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