TY - JOUR
T1 - Cloning, purification, crystallization and preliminary crystallographic analysis of SecA from Enterococcus faecalis
AU - Meining, Winfried
AU - Scheuring, Johannes
AU - Fischer, Markus
AU - Weinkauf, Sevil
PY - 2006/6
Y1 - 2006/6
N2 - 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, α = γ = 90.0, β = 119.1°. A selenomethionine derivative was prepared and is currently being tested in crystallization trials.
AB - 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, α = γ = 90.0, β = 119.1°. A selenomethionine derivative was prepared and is currently being tested in crystallization trials.
UR - http://www.scopus.com/inward/record.url?scp=33745127322&partnerID=8YFLogxK
U2 - 10.1107/S1744309106017544
DO - 10.1107/S1744309106017544
M3 - Article
C2 - 16754988
AN - SCOPUS:33745127322
SN - 1744-3091
VL - 62
SP - 583
EP - 585
JO - Acta Crystallographica Section F: Structural Biology and Crystallization Communications
JF - Acta Crystallographica Section F: Structural Biology and Crystallization Communications
IS - 6
ER -