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Protein Science, Vol 5, Issue 3 538-541, Copyright © 1996 by Cold Spring Harbor Laboratory Press

FOR THE RECORD

Crystallization and preliminary diffraction studies of NodL, a rhizobial O-acetyl-transferase involved in the host-specific nodulation of legume roots

S. M. DUNN, PCE. MOODY, J. A. DOWNIE and W. V. SHAW
Department of Biochemistry, University of Leicester, Adrian Building, University Road, Leicester LE1 7RH, UK Present address: Department of Biochemistry and Physiology, IACR-Rothamsted, Harpenden, Herts AL5 2JQ, UK.

The NodL specified O-acetyltransferase from the microbial symbiont Rhizobium leguminosarum has been over-expressed in Escherichia coli and purified using affinity-elution dye chromatography as the key step. The protein has been crystallized at 20{deg}C in 18% PEG 600, 0.1 M Tris/HCl buffer, pH 8.5, containing 1% dioxane, 0.25% octyl-{beta}-glucoside, and 5 mM coenzyme A using the hanging drop vapor diffusion method. Ambient temperature X-ray diffraction studies reveal the space group to be hexagonal (P6(3)22) with lattice constants a = b = 77.08 A, c = 160.6 A, and {alpha} = {beta} = 90{deg}, {gamma} = 120{deg}. Crystals that are flash-frozen to 120 K diffract beyond 2.7 A.
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