Abstract
Crystals of recombinant NovN, an O-carbamoyltransferase from Streptomyces spheroides, were grown by vapour diffusion. The protein crystallized in two different crystal forms. Crystal form I belonged to space group C2 and native data were collected to 2.9 Å resolution in-house. Crystal form II had I-centred orthorhombic symmetry and native data were recorded to a resolution of 2.3 Å at a synchrotron. NovN catalyses the final step in the biosynthesis of the aminocoumarin antibiotic novobiocin that targets the essential bacterial enzyme DNA gyrase. © 2008 International Union of Crystallography All rights reserved.
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Gómez García, I., Freel Meyers, C. L., Walsh, C. T., & Lawson, D. M. (2008). Crystallization and preliminary X-ray analysis of the O- carbamoyltransferase NovN from the novobiocin-biosynthetic cluster of Streptomyces spheroides. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 64(11), 1000–1002. https://doi.org/10.1107/S1744309108030145
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