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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Crystallization and preliminary X-ray analyses of catabolite control protein A, free and in complex with its DNA-binding site.

The catabolite control protein (CcpA) from Bacillus megaterium is a member of the bacterial repressor protein family GalR/LacI. CcpA with an N-terminal His-tag was used for crystallization. Crystals of free CcpA and of CcpA in complex with the putative operator sequence (catabolite responsive elements, CRE) were obtained by vapour-diffusion techniques at 291 K using the hanging-drop method. CcpA crystals grown in the presence of polyethylene glycol 8000 belong to the hexagonal space group P6(1)22 or P6(5)22, with unit-cell parameters a = 74.4, c = 238.8 A. These crystals diffract X-rays to 2.55 A resolution and contain one monomer of the homodimeric protein per asymmetric unit. Crystals of the CcpA-CRE complex were obtained with ammonium sulfate as precipitant and belong to the tetragonal space group I4(1)22, with unit-cell parameters a = 125, c = 400 A and one complex per asymmetric unit. Although these co-crystals grew to a sufficient size, X-ray diffraction was limited to 8 A resolution.[1]

References

  1. Crystallization and preliminary X-ray analyses of catabolite control protein A, free and in complex with its DNA-binding site. Tebbe, J., Orth, P., Küster-Schöck, E.K., Hillen, W., Saenger, W., Hinrichs, W. Acta Crystallogr. D Biol. Crystallogr. (2000) [Pubmed]
 
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