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Title
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Crystallization and preliminary X-ray diffraction analysis of ScrY, a specific bacterial outer membrane porin.
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Authors
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D.Forst,
K.Schülein,
T.Wacker,
K.Diederichs,
W.Kreutz,
R.Benz,
W.Welte.
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Ref.
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J Mol Biol, 1993,
229,
258-262.
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PubMed id
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Abstract
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The sucrose-specific outer membrane porin ScrY of Salmonella typhimurium was
isolated from Escherichia coli K-12 strain KS 26 containing the plasmid pPSO112.
The protein was purified to homogeneity by differential extraction of the cell
envelope in the presence of the detergents sodium dodecyl sulfate and lauryl
(dimethyl)-amine oxide (LDAO). The porin had apparent molecular weights of 58
kDa and 120 kDa for the monomer and for the trimer, respectively, on SDS/PAGE.
The purified trimers were crystallized using poly(ethylene glycol) 2000 and the
detergents octylglucoside (OG) and hexyl-(dimethyl)-amine oxide (C6DAO). X-ray
diffraction of the crystals showed reflections to 2.3 A. The space group of the
crystals was R3 and the lattice constants of the hexagonal axes were a = b =
112.85 A and c = 149.9 A. The crystal volume per unit of protein molecular
weight was 3.47 A3/Da.
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