Volume 54, Issue 6-2 pp. 1416-1418

Crystallization and preliminary X-ray studies of the Rhizobium meliloti DctD two-component receiver domain

Mark Staley

Mark Staley

Department of Biochemistry and Molecular Biology, 108 Althouse Laboratory, The Pennsylvania State University, University Park, PA 16802, USA

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Lori C. Zeringue

Lori C. Zeringue

Department of Biochemistry and Molecular Biology, 108 Althouse Laboratory, The Pennsylvania State University, University Park, PA 16802, USA

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Richard D. Kidd

Richard D. Kidd

Department of Biochemistry and Molecular Biology, 108 Althouse Laboratory, The Pennsylvania State University, University Park, PA 16802, USA

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B. Tracy Nixon

B. Tracy Nixon

Department of Biochemistry and Molecular Biology, 108 Althouse Laboratory, The Pennsylvania State University, University Park, PA 16802, USA

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Gregory K. Farber

Gregory K. Farber

Department of Biochemistry and Molecular Biology, 108 Althouse Laboratory, The Pennsylvania State University, University Park, PA 16802, USA

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First published: 27 September 2007

Abstract

The Rhizobium meliloti DctD two-component receiver domain was expressed in Escherichia coli and purified to homogeneity. Crystals were obtained using the hanging-drop vapor-diffusion geometry with ammonium phosphate as the precipitant. The crystals diffract to 2.3 Å and exhibit the symmetry of space group I222 or I212121. The unit-cell dimensions are a = 59.0, b = 58.6 and c = 169.8 Å. The asymmetric unit contains a dimer and the crystals have a Vm of 2.16 Å3 Da−1.

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