Overexpression, purification and crystallization of the tetrameric form of SorC sorbitol operon regulator.
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.
de Sanctis
Daniele
D
Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Avenida da República, Apartado 127, 2781-901 Oeiras, Portugal.
Rêgo
Ana T
AT
Marçal
David
D
McVey
Colin E
CE
Carrondo
Maria A
MA
Enguita
Francisco J
FJ
D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray; D007711:Klebsiella pneumoniae / Q000235:genetics*; D046911:Macromolecular Substances / Q000737:chemistry; D009876:Operon; D016133:Polymerase Chain Reaction; D011994:Recombinant Proteins / Q000737:chemistry* / Q000302:isolation & purification; D013012:Sorbitol / Q000378:metabolism*; D013013:Sorbose / Q000378:metabolism; D015534:Trans-Activators / Q000737:chemistry*; D014961:X-Ray Diffraction
D001426:Bacterial Proteins; D046911:Macromolecular Substances; D011994:Recombinant Proteins; D015534:Trans-Activators; D013012:Sorbitol; D013013:Sorbose