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Overexpression, purification and crystallization of the tetrameric form of SorC sorbitol operon regulator.

ABSTRACT: The sorbitol operon regulator (SorC) regulates the metabolism of L-sorbose in Klebsiella pneumonia. SorC was overexpressed in Escherichia coli and purified, and crystals were obtained of a tetrameric form. A single crystal showed X-ray diffraction to 3.20 A. The crystal belongs to space group P2(1)2(1)2(1), with unit-cell parameters a = 91.6, b = 113.3, c = 184.1 A. Analysis of the molecular-replacement solution indicates the presence of four SorC molecules in the asymmetric unit.

SUBMITTER: de Sanctis D

PROVIDER: S-EPMC2373991 | biostudies-literature | 2008 Jan

REPOSITORIES: biostudies-literature

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Overexpression, purification and crystallization of the tetrameric form of SorC sorbitol operon regulator.

de Sanctis Daniele D Rêgo Ana T AT Marçal David D McVey Colin E CE Carrondo Maria A MA Enguita Francisco J FJ

Acta crystallographica. Section F, Structural biology and crystallization communications 20071220 Pt 1

The sorbitol operon regulator (SorC) regulates the metabolism of L-sorbose in Klebsiella pneumonia. SorC was overexpressed in Escherichia coli and purified, and crystals were obtained of a tetrameric form. A single crystal showed X-ray diffraction to 3.20 A. The crystal belongs to space group P2(1)2(1)2(1), with unit-cell parameters a = 91.6, b = 113.3, c = 184.1 A. Analysis of the molecular-replacement solution indicates the presence of four SorC molecules in the asymmetric unit. ...[more]

PMID: 18097095

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