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The C-terminal truncated form of the S-layer protein SbsC from Geobacillus stearothermophilus, rSbsC31–844, has been crystallized by the vapour-diffusion method using polyethylene glycol 6000 as a precipitating agent. The crystals diffract to 3 Å resolution using synchrotron radiation and belong to space group P21, with unit-cell parameters a = 57.24, b = 98.91, c = 108.62 Å, β = 94.34°. One molecule is present in the asymmetric unit, which corresponds to a solvent content of 65%. Native and heavy-atom derivative data have been collected. The Pt derivative yielded two high-occupancy sites per molecule.

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