Abstract
DtsR1, a carboxyltransferase subunit of acetyl-CoA carboxylase derived from Corynebacterium glutamicum, was crystallized by the sitting-drop vapour-diffusion method using polyethylene glycol 6000 as a precipitant. The crystal belongs to the trigonal system with space group R32 and contains three subunits in the asymmetric unit. A molecular-replacement solution was found using the structure of transcarboxylase 12S from Propionibacterium shermanii as a search model. © International Union of Crystallography 2007.
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Yamada, M., Natsume, R., Nakamatsu, T., Horinouchi, S., Kawasaki, H., & Senda, T. (2007). Crystallization and preliminary crystallographic analysis of DtsR1, a carboxyltransferase subunit of acetyl-CoA carboxylase from Corynebacterium glutamicum. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 63(2), 120–122. https://doi.org/10.1107/S1744309107001078
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