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Updated: May 16, 2026

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae
Published on: January 10, 2018
Crystallization of domains involved in self-assembly of the S-layer protein SbsC
Anđela Ðordić1, Eva M Egelseer, Manfred Tesarz
1Institute of Molecular Biosciences, Karl-Franzens University Graz, Humboldtstrasse 50, 8010 Graz, Austria.
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.
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