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

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Expression, purification and crystallization of enterococcus faecium streptogramin A acetyltransferase.

The streptogramin A acetyltransferase from Enterococcus faecium (SWISS-PROT P50870) has been overexpressed in Escherichia coli, purified and crystallized. Crystallization conditions were screened using the hanging-drop vapor-diffusion method and resulted in two distinct crystal forms. Form I crystals diffract to 2.5 A and belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 68.6, b = 102.6, c = 107.5 A. Form II crystals diffract to 2.7 A and belong to space group F222, with unit-cell parameters a = 185.8, b = 185.8, c = 186.5 A. Rotation-function and packing analyses for both crystal forms indicate that the asymmetric unit may contain one and two copies of the trimeric enzyme for crystal forms I and II, respectively.[1]

References

  1. Expression, purification and crystallization of enterococcus faecium streptogramin A acetyltransferase. Sugantino, M., Roderick, S.L. Acta Crystallogr. D Biol. Crystallogr. (2000) [Pubmed]
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