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

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Crystallization and preliminary crystallographic analysis of formyl-CoA tranferase from Oxalobacter formigenes.

Formyl-CoA transferase from Oxalobacter formigenes has been expressed as a recombinant protein in Escherichia coli and purified to homogeneity. Crystals of formyl-CoA transferase were grown at 293 K using polyethylene glycol 4000 as a precipitant. The diffraction pattern of flash-frozen crystals at 100 K extends to 2.2 A resolution with synchrotron radiation (lambda = 0.933 nm). The crystals are tetragonal and belong to space group I4, with unit-cell parameters a = b = 151.44, c = 99.49 A. The asymmetric unit contains one dimer and the solvent content is 53%. Formyl-CoA transferase was crystallized both as the apoenzyme and as its complex with coenzyme A.[1]

References

  1. Crystallization and preliminary crystallographic analysis of formyl-CoA tranferase from Oxalobacter formigenes. Ricagno, S., Jonsson, S., Richards, N., Lindqvist, Y. Acta Crystallogr. D Biol. Crystallogr. (2003) [Pubmed]
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