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Updated: Aug 6, 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
Cloning, purification and preliminary crystallographic analysis of a conserved hypothetical protein, SA0961 (YlaN),
Ling Xu1, Svetlana E Sedelnikova, Patrick J Baker
1Krebs Institute for Biomolecular Research, Department of Molecular Biology and Biotechnology, The University of Sheffield, Sheffield S10 2TN, England.
Abstract:
SA0961 is an unknown hypothetical protein from Staphylococcus aureus that can be identified in the Firmicutes division of Gram-positive bacteria. The gene for the homologue of SA0961 in Bacillus subtilis, ylaN, has been shown to be essential for cell survival, thus identifying the protein encoded by this gene as a potential target for the development of novel antibiotics. SA0961 was cloned and the protein was overexpressed in Escherichia coli, purified and subsequently crystallized. Crystals of selenomethionine-labelled SA0961 diffract to beyond 2.4 angstroms resolution and belong to the monoclinic space group P2(1), with unit-cell parameters a = 31.5, b = 42.7, c = 62.7 angstroms, beta = 92.4 degrees and two molecules in the asymmetric unit. A full structure determination is under way to provide insights into the function of this protein.
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