Acta Crystallographica Section F

Structural Biology and Crystallization Communications

Volume 62, Part 6 (June 2006)

crystallization communications


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Acta Cryst. (2006). F62, 583-585    [ doi:10.1107/S1744309106017544 ]

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

W. Meining, J. Scheuring, M. Fischer and S. Weinkauf

Abstract: 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 Å 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 Å, [alpha] = [gamma] = 90.0, [beta] = 119.1°. A selenomethionine derivative was prepared and is currently being tested in crystallization trials.

Keywords: SecA; Enterococcus faecalis.

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