Abstract
Dihydrodipicolinate synthase (DHDPS; EC 4.2.1.52) catalyzes the first committed step of the lysine-biosynthetic pathway in plants and bacteria. Since (S)-lysine biosynthesis does not occur in animals, DHDPS is an attractive target for rational antibiotic and herbicide design. Here, the cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of DHDPS2 from Arabidopsis thaliana are reported. Diffraction-quality protein crystals belonged to space group P21212. © 2011 International Union of Crystallography. All rights reserved.
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Griffin, M. D. W., Billakanti, J. M., Gerrard, J. A., Dobson, R. C. J., & Pearce, F. G. (2011). Crystallization and preliminary X-ray diffraction analysis of dihydrodipicolinate synthase 2 from Arabidopsis thaliana. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 67(11), 1386–1390. https://doi.org/10.1107/S1744309111033276
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