Cloning, purification, crystallization and preliminary crystallographic analysis of SecA from Enterococcus faecalis.

نویسندگان

  • Winfried Meining
  • Johannes Scheuring
  • Markus Fischer
  • Sevil Weinkauf
چکیده

The gene coding for SecA from Enterococcus faecalis was cloned and overexpressed in Escherichia coli. In this protein, the lysine at position 6 was replaced by an asparagine in order to reduce sensitivity towards proteases. The modified protein was purified and crystallized. Crystals diffracting to 2.4 A resolution were obtained using the vapour-diffusion technique. The crystals belong to the monoclinic space group C2, with unit-cell parameters a = 203.4, b = 49.8, c = 100.8 A, alpha = gamma = 90.0, beta = 119.1 degrees. A selenomethionine derivative was prepared and is currently being tested in crystallization trials.

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عنوان ژورنال:
  • Acta crystallographica. Section F, Structural biology and crystallization communications

دوره 62 Pt 6  شماره 

صفحات  -

تاریخ انتشار 2006