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

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

A large compressibility change of protein induced by a single amino acid substitution.

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

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Downie, J. A. Shaw, W. V. Dunn, S. M. Moody, P. C.
Description	Country affiliation: United kingdom Author Affiliation: Dunn SM ( Department of Biochemistry, University of Leicester, UK.)
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.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	3
Volume Number	5
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	1996-03-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Acetyltransferases Chemistry Bacterial Proteins Rhizobium Leguminosarum Enzymology Amino Acid Sequence Binding Sites Genetics Carbohydrate Sequence Coenzyme A Metabolism Crystallization Crystallography, X-ray Escherichia Coli Gene Expression Molecular Sequence Data Recombinant Proteins Sequence Alignment Research Support, Non-u.s. Gov't Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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