Abstract
The crystal structure of the hypothetical protein YqgQ from Bacillus subtilis has been determined to 2.1 Å resolution. The crystals belonged to space group P21, with unit-cell parameters a = 51.85, b = 41.25, c = 55.18 Å, Β = 113.4°, and contained three protein molecules in the asymmetric unit. The structure was determined by the single-wavelength anomalous dispersion method using selenium-labeled protein and was refined to a final R factor of 24.7% (Rfree = 28.0%). The protein molecule mainly comprises a three-helical bundle. Its putative function is inferred to be single-stranded nucleic acid binding based on sequence and structural homology. © 2010 International Union of Crystallography All rights reserved.
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CITATION STYLE
Lakshminarasimhan, D., Eswaramoorthy, S., Burley, S. K., & Swaminathan, S. (2009). Structure of YqgQ protein from Bacillus subtilis, a conserved hypothetical protein. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 66(1), 8–11. https://doi.org/10.1107/S1744309109047009
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