Please use this identifier to cite or link to this item: http://hdl.handle.net/2381/25025
Title: Crystallization and preliminary diffraction studies of NodL, a rhizobial O-acetyl-transferase involved in the host-specific nodulation of legume roots.
Authors: Dunn, SM
Moody, PC
Downie, JA
Shaw, WV
First Published: Mar-1996
Citation: PROTEIN SCI, 1996, 5 (3), pp. 538-541
Abstract: 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 degrees 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 degrees, gamma = 120 degrees. Crystals that are flash-frozen to 120 K diffract beyond 2.7 A.
DOI Link: 10.1002/pro.5560050318
ISSN: 0961-8368
Links: http://hdl.handle.net/2381/25025
Type: Journal Article
Appears in Collections:Published Articles, Dept. of Biochemistry

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